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At present, there have been many molecular modifications for alginate, mainly focused on site directed mutagenesis and domain recombination. For example, Lu et al. obtained a mutant with a 75.80% increase in enzyme activity compared to the wild type through site mutagenesis[8]. Zhang et al. obtained a mutant with enzyme activity 2.35 times higher than the wild-type through domain recombination[9]. However, the use of error prone PCR for the modification of alginate enzymes is still limited. Li et al. used error prone PCR technology to increase the activity of alginate, causing enzyme activity to be 2.41 times higher than before [10]. Our experiments have confirmed the significant potential of error prone PCR to modify alginate enzyme activity, which can be applied to improve alginate enzyme activity, increase alginate oligosaccharide production, and meet industrial needs.

Alginate oligosaccharides have extremely high value, and their main production method is still the degradation of alginate by alginate enzymes. Wild type enzymes often have low activity. However, there are still not many highly active alginate enzymes that have been artificially modified. This experiment is a beneficial attempt. We hope to use error prone PCR technology to modify and obtain more highly active alginate enzymes in the future.

In the experiment, we noticed some issues that need to be studied and improved. Alginate cannot self color and lacks the necessary identification markers for high-throughput screening. The traditional DNS method is slightly cumbersome, and the method we use to detect the amount of product using the value of OD235 is relatively simple. However, the value of OD235 is difficult to accurately quantify the product. It can only be used for comparison, indicating that the activity of the mutant is higher than that of the wild type. In addition, this method may be affected by some interfering factors. 

Due to the reaction characteristics, the electrophoretic bands of error-prone PCR products are not very bright, and sometimes there was not enough product which can be recovered. Our strategy is to conduct PCR reactions on multiple tubes simultaneously. 

During the dry lab, site-directed mutagenesis yielded the R30W variant, which demonstrated enhanced enzymatic activity relative to the 5ZU5 construct. This increase in activity may be attributed to the fact that, despite the molecular docking scores remaining invariant between R30W and 5ZU5, the number of binding sites with sodium alginate for R30W has been augmented. An increased number of binding sites could potentially amplify the intermolecular interactions between the protein and its ligand, culminating in a heightened binding affinity and, consequently, an elevation in the protein's bioactivity. 

We also encountered the issue of inconsistent standards for the activity of alginate enzymes. We attempt to construct a model that can predict the enzyme activity of a specific sequence encoding alginate enzymes. However, the inconsistent enzyme activity measurement standards in the papers have posed difficulties for our attempts to construct models. We hope to develop a unified and easily measurable standard to measure the activity of alginate enzymes.




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Reference

[1]Cheng D, Jiang C, Xu J, et al. Characteristics and applications of alginate lyases: A review[J]. International Journal of Biological Macromolecules, 2020, 164: 1304-1320. 

DOI：https://doi.org/10.1016/j.ijbiomac.2020.07.199

[2] A La Teng Zhu La, Hu YF. Advances in the preparation of alginate oligosaccharides and its biological functions. Chinese Journal of Biotechnology, 2022, 38(1): 104-118.

DOI: https://dx.doi.org/10.13345/j.cjb.210377

[3] HAN Yang, WANG Shujing.The anti-tumor effect of brown algae polysaccharide and its derivatives[J]. Chemistry of Life,2019(04):673-680.

DOI: https://dx.doi.org/10.13488/j.smhx.20180130

[4] Palackal N, Brennan Y, Callen W N, et al. An evolutionary route to xylanase process fitness[J]. Protein science, 2004, 13(2): 494-503. 

DOI：https://doi.org/10.1110/ps.03333504

[5] Wang Y, Fu Z, Huang H, et al. Improved thermal performance of Thermomyces lanuginosus GH11 xylanase by engineering of an N-terminal disulfide bridge[J]. Bioresource Technology, 2012, 112(5): 275–279. 

DOI：https://doi.org/10.1016/j.biortech.2012.02.092

[6] Zhang K, Liu T, Liu W, et al. Structural insights into the substrate-binding cleft of AlyF reveal the first long-chain alginate-binding mode[J]. Acta Crystallographica Section D: Structural Biology, 2021, 77(3): 336-346.

DOI：https://doi.org/10.1107/s205979832100005x

[7] Zhang Hongxiu, Liu Xiaohua, Liu Weizhi. Study on the New Alginate Lyase AlyPC1 from Marine Bacterium Pseudoalteromonas sp. 01[J].Periodical of Ocean University of China,2024,54(02):84-88+105. 

DOI：http://dx.doi.org/10.16441/j.cnki.hdxb.20220128

[8]Lu Y, Zhou J, Gu Q, et al. Cloning, expression and improvement of catalytic activity of alginate lyase by site-directed mutation[J]. Systems Microbiology and Biomanufacturing, 2022, 2(3): 555-567.

DOI：https://doi.org/10.1007/s43393-022-00084-w

[9]Zhang Z, Tang L, Bao M, et al. Functional characterization of carbohydrate-binding modules in a new alginate lyase, TsAly7B, from Thalassomonas sp. LD5[J]. Marine drugs, 2019, 18(1): 25. 

DOI：https://doi.org/10.3390/md18010025

[10] Li Shu,Zhang Wei,Zhao Chunmei.Directed Evolution of Alginate Lyase Alg-2 Based on Error Prone PCR[J].Food Science,2019(04):146-151.

DOI：http://dx.doi.org/10.7506/spkx1002-6630-20180207-100

[11] Qianqian Lyu, Keke Zhang, Qiaoyun Zhu, Zhijian Li, Yujie Liu, Elisabeth Fitzek, Tanner Yohe, Liming Zhao, Weihua Li, Tao Liu, Yanbin Yin, Weizhi Liu. Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes, Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1862, Issue 9, 2018, Pages 1862-1869, ISSN 0304-4165

DOI: https://doi.org/10.1016/j.bbagen.2018.05.024


Acknowledgment

Throughout the writing of this dissertation, we have received a great deal of support and assistance. We would first like to thank our supervisor, Prof. Weizhi Liu, whose expertise was invaluable in formulating the research questions and methodology.Your insightful feedback pushed us to sharpen our thinking and brought our work to a higher level.

We would especially like to thank our advisor, Junyi Huang, who provided meticulous assistance throughout the entire process of our experiment. Without his guidance, it would not have been possible for us to complete the experiment successfully.

We would particularly like to acknowledge all of our team members, for their wonderful collaborationand persistent efforts.

We would also like to express our gratitude to WeihaoZhou as well asother graduate studentsin the lab, who provided extremely valuable guidance on the operational details of this experiment, ensuring the progress of our work.

We are grateful to our classmates, the 2024 iGEM team, OUC_China for lending us important laboratory equipment.

Finally,we also would like to express our sincere gratitude to our college--College of Marine Life Sciences, Ocean University of Chinafor providing us with the venue and experimental reagents,and encouragingus to successfully complete ourresearch. We are grateful to Professor XianghongWang forhis efforts in supplementing the experimental materials.

OUC_DE Author List_2024.pdf

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1. Wet Lab

1.1 Plasmid and strain

We used E.coli BL21(DE3)(provided by our instructor's lab) as recipient and pET32a vector which contains an ampicillin resistance gene as the selection marker.

1.2 Extraction of pET32a-AlyAYO plasmid and double enzyme digestion

Inoculate 50 µL of glycerol bacteria(provided by our instructor's lab) into 5 mL of LB liquid medium(HB0128, hopebio) containing a one-thousandth concentration of ampicillin(Sangon biotech) and incubate overnight at 37℃ and 180rpm on a constant temperature shaker(MQL-61R, Shanghai Minquan Instrument Co., Ltd). The plasmid was extracted with a plasmid extraction kit (E.Z.N.A. Plasmid DNA Mini Kit Ⅰ, V spin, Omega Bio-Tek). The concentration and quality of the extracted plasmids were detected by Nano Drop (Thermo Scientific Nanodrop One).

Then we produced double enzyme digestion to collect pET32a linearized plasmid and AlyAYO gene. The reaction system was set as Table 1.

Table 1 Composition of Plasmid Extraction Reaction Mixture

Reagent Name

Dosage(μL)

plasmid

45

BamHⅠ

1.5

XhoⅠ

1.5

10× K Buffer

5.3

The reaction was performed at 30℃ for at least 6h. The product was examined by 1% agarose (1110GR100, Biofroxx ) gel electrophoresis and then recovered with gel extraction kit (E.Z.N.A. Gel Extraction Kit V spin, Omega Bio-Tek).

1.3 Error-prone PCR

The PCR primers were designed with the intention of introducing errors, using the following parameters: primer F of GGATCCATGGCGCAGCTGGACCCGA and an annealing temperature of 70.9℃; primer R of CTCGAGTTAGTGTTTGATATCCAGCTGGTAGAAGCTAACCTGG and annealing temperature of 65.9℃. The error-prone PCR was carried out using Error-prone PCR kit (Controlled Error-prone PCR Kit (ZY-160903), Zebra Bio), the template was the extracted plasmid, and the two mutation numbers of 5,8 were selected and 35 cycles were carried out for 4 times.

The reaction systems with AlyAYO template concentrations of 1ng/μL and 10ng/μL were set as Table 2.

Table 2 Composition of Error-prone PCR Reaction Mixture

expected number of mutations per 1000bp

5

8

5× Mix

6μl

6μl

MnCl2

4μl

4μl

dGTP

1μl

4μl

template

1μl

1μl

pF

1μl

1μl

pR

1μl

1μl

DNA polymerase

0.5μl

0.5μl

ddH2O

15.5μl

12.5μl


After pre-denaturation at 94℃ for 3min, 35 cycles of reaction were performed: denaturation at 94℃for 1 min, annealing at 60.9℃ for 1 min and extension at 72℃ for 3min(A300 Fast Thermal Cycler，LongGene). The PCR products were examined by electrophoresis on 1% agarose gel.

1.4 Double digestion and agarose gel electrophoresis for product recovery

Cycle-pure Kit (E.Z.N.A. Cycle-pure Kit(D6492-02), Omega Bio-Tek) was then used to recover the mutated AlyAYO gene from the product of error-prone PCR. Then the mutated genes were subjected to digestion with two enzymes(BamHⅠ(1010S) and XhoⅠ(1094S), Takara) and K Buffer(Takara, comes with BamHⅠ enzyme). Add 1.5μl of each enzyme, and the amount of K Buffer added is one tenth of the total system. Agarose gel electrophoresis was then performed to recover the mutated AlyAYO gene using an agarose gel recovery kit (E.Z.N.A. Gel Extraction Kit V spin, Omega Bio-Tek). The digested products were incubated at 30°C for at least 6 hours. The concentration and quality of the recovered products were subsequently determined using a Nano Drop spectrophotometer (Thermo Scientific NanoDrop one).

1.5 Connections and conversions

The mutant gene and pET32a plasmid which had been digested into a linear form by two enzyme should be connected together.

The connecting reaction system was set as Table 3.

Table 3 Composition of Connecting Reaction Mixture

Reagent Name

Dosage(μL)

gene

7

vector

1

T4 DNA Ligase (2011A, Takara)

1

T4 DNA Ligase Buffer (Takara, comes with T4 DNA Ligase)

1


The ligation process should be carried out for a minimum of four hours at 16°C.

The ligation product should be added to the receptor cell, and the volume of the ligation product should not exceed 1/10 of the receptor cell. The mixture should be gently agitated, incubated on ice for 30 minutes, and then heated to 42°C for 90 seconds without agitation. Subsequently, the mixture was immediately transferred to an ice water bath for 2-3 minutes, after which 900 μL of Amp-free LB medium was added. The bacteria were then incubated in a constant temperature shaker with oscillation at 37°C and 150 rpm for 45 minutes. A 45-minute incubation period is required for the bacterium to revive and for the resistance gene to be expressed. Centrifugation at 2500 g for 5 minutes is then performed, after which the supernatant of 900μL is aspirated. The bacterium is then resuspended in the remaining medium and spread uniformly on the resistance plate with a sterile applicator stick. Once the bacterial liquid has been absorbed by the plate, it is incubated inverted at 37°C overnight. At the same time, the unmutated wild-type bacterial fluid is used to delineate the control group.

1.6 96-well plate culture and induction

A volume of 150μl of Amp-containing LB medium should be added to each well of a 96-well plate(96-well Clear Flat Bottom UV-Transparent Microplate, corning). The colonies should then be picked from the plate and transferred into the wells, where they should be incubated at 37°C 180 rpm with oscillation until the true absorbance of the bacterial solution reaches 0.6-0.8. The true absorbance is defined as follows: true absorbance = (measured absorbance – blank absorbance) x 1.3125. Because the optical path length of our enzyme-linked immunosorbent assay (ELISA) reader is different from the one used in the paper we referenced. Before induction, we take 25μL of bacterial solution from each well and transfer it to another 96-well plate. After continuing to culture for several hours, we add an equal volume of 30% glycerol(10010618, Shanghai Hushi Laboratory Equipment Co., Ltd) for seed preservation. The remaining bacterial solution should then be supplemented with the appropriate amount of IPTG(Sangon Biotech) to achieve the desired working concentration（0.2mmol/L）. The culture was incubated in a constant temperature shaker set at 16°C with an agitation speed of 180 rpm for a period of 18 to 20 hours.[6,7]

1.7 Detection of enzyme activity

The bacterial precipitate should be obtained by centrifuging the 96-well plate at 4000 rpm. A volume of 150μl of bacterial lysate should be added to each well, after which the plate should be incubated at 37°C in a constant temperature incubator for one hour. Subsequently, 190μl of substrate solution should be added to the UV 96-well plate, and the contents should be suctioned. The substrate solution contains 0.2% sodium alginate(Shanghai Yuanye Bio-Technology Co., Ltd), 50mM Tris HCl(self-made by Tris and HCl, Tris was from Biofroxx, 1115GR500) solution with pH 7.5, and 200mM NaCl(10019318, Shanghai Hushi Laboratory Equipment Co., Ltd). A volume of 10μl of the diluted enzyme solution (enzyme solution: diluted buffer = 2:3, the composition of the diluted buffer is the same as the substrate solution but does not contain sodium alginate) should be added to the substrate solution with a row gun. The solution should be mixed gently to prevent the formation of bubbles and then the Bio-Tek Epoch Microplate Spectrophotometer should be used to determine the 235 nm wavelength absorbance.

2. Dry Lab

2.1 Protein obtaining, imitating, docking and analyzing

First, we obtained the 5ZU5 protein sequence from PDB[11], which was later analyzed in detail. Using BLAST(Basic Local Alignment Search Tool) on the National Center for Biotechnology Information website, protein sequences that shared no less than 90% similarities with 5ZU5 protein sequence were selected. Respectively, Consensus Finder and CB-Dock helped us with analyzing several highly conserved sites and identifying the binding sites where proteins and alginate interact. We then performed site-directed mutagenesis on those regions. We used Alphafold 3 to generate the structure of mutant proteins, performed molecular docking and analyzed the results. Since CB-Dock uses blind docking as its protein docking strategy, which led to the possibility of substrates binding to different regions, we calculated the potential substrate pocket area to ensure that substrates and enzymes bound at the correct sites. Additionally, the binding affinity of certain protein docking interactions was analyzed to determine whether it was acceptable.


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1.Wet Lab

1.1 error-prone PCR 

The alginate gene we modified was AlyAYO, with a total length of 930bp. We cultured E. coli BL21 containing pET32a-AlyAYO plasmids from its glycerol stock which is from Marine Enzyme Laboratory of Ocean University of China and extracted pET32a-AlyAYO plasmids. Then, we digested pET32a-AlyAYO plasmids with BamHⅠand XhoⅠ to collect pET32a plasmid and AlyAYO gene, which were expression vector and the template of error-prone PCR.

Controlled error-prone PCR Kit (No. ZY-160903) was used to preform sequential error-prone PCR on AlyAYO. The set of number of cycles was 35. The expected mutation values are set to 5 per 1000bp and 8 per 1000bp. In each tube, 5μL of 30μl product was used for agarose gel electrophoresis. The results of error-prone PCR products after agarose gel electrophoresis are shown in Fig1.

Fig1 Product electrophoresis results

M: Marker2000

1: Error-prone PCR products with a concentration of 10ng/μL as template and the expected mutation value is set to 5 per 1000bp

2: Error-prone PCR products with a concentration of 1ng/μL as template and the expected mutation value is set to 5 per 1000bp

3: Error-prone PCR products with a concentration of 10ng/μL as template and the expected mutation value is set to 8 per 1000bp

4: Error-prone PCR products with a concentration of 1ng/μL as template and the expected mutation value is set to 8 per 1000bp

1.2 Construction of expression vector

The remaining product was digested sequentially with BamHⅠand XhoⅠ. Then we ligated error-prone PCR product into the corresponding sites of the pET32a plasmid to construct the vector and the vector was transformed into E. coli BL21 which was self-made by Marine Enzyme Laboratory of Ocean University of China. 

1.3 Enzymatic activity analysis of expressed proteins

We picked single colonies which are successfully transformed and cultured them in 96 well plates. After induction with IPTG, we lysed the cells, used the supernatant as the crude enzyme solution, and measured the enzyme activity. 

One unit of enzyme activity was defined as an increase of 1 OD235 unit per min. The enzyme activity of original strain was 12.350U/ml. Among the 32 mutant strain, the enzyme activity of some of them have significantly increased, which are shown as follows. The enzyme activity of the mutant with the highest activity is more than three times that of the wild type. 

Fig2 The enzyme activity of original strain and its mutant strains.


2. Dry Lab

2.1 A positively mutant protein R30W

Finally, we obtained a positively mutant protein R30Wwhose amino acid sequence is GPPDLGTDDDDKAMADIASDFPNNKETGEALLTPVDATASSHDGNGPDWLIDQDLTTRWSSAGDGEWAMLDYGSVQEFDAVQASFSKGNERQSKFDIQVSVDGETWTTVLENQLSSGKAIGLERFQFEPAVKARYVRYVGHGNTKNGWNSVTGLAAVNCSINACPASQIITSDVVAAEAVLIAEMKAAEKARKAARKDLRSGNFGVAAVYPCETSVKCDTRSALPVPTGLPATPVAGNAPSENFDMTHWYLSQPFDHDKNGKPDDVSEWNLANGYQHPEIFYTADDGGLVFKSYVKGVRTSKNTKYARTELREMMRRGDQSISTKGVNKNNWVFSSAPEADLEAAAGIDGVLEATLKIDHATTTGNANEVGRFIIGQIHDQNDEPIRLYYRKLPNQPTGAVYFAHESQDATKEDFYPLVGDMTAEVGEDGIALGEVFSYRIDVKGNTMTVTLMREGKDDVVQVVDMSNSGYDVGGKYMYFKAGVYNQNISGDLDDYSQATFYQLDVSHDQYKK. Compared with 5ZU5, the docking score of R30W has not changed, but the number of binding sites with sodium alginate has increased from 25 to 37. More binding sites may enhance the interaction between protein and ligand, resulting in enhanced binding affinity, thereby improving the biological activity of the protein. The 3D docking molecule structure of the R30W is shown in Figure 3.

Fig3The 3D docking molecule structure of the R30W.

The amino acids marked in purple in the figure are the amino acids that bind to the substrate, which are ASP36, ALA37, THR38, ALA39, HIS42, ASP43, GLY44, ASN45, GLY46, PRO47, ASP48, TRP49, LYS305, TYR306, THR363, ALA367, ASN368, GLU369, VAL370, ARG372, ILE374, ARG387, TYR389, ARG391, LEU393, PRO394, ASN395, GLN396, TYR402, ALA404, GLU413, PHE415, MET422, THR423, GLU425, TYR485, GLN487.


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+ Alginate oligosaccharides have found extensive applications in the fields of food, healthcare, and biomedicine. Alginate lyase serves as the primary tool for the preparation of alginate oligosaccharides. Thus, the identification of alginate lyases with high enzymatic activity is of significant importance. However, the activity of wild-type alginate lyases is often insufficient for practical applications. Therefore, engineering alginate lyases at the molecular level to enhance their activity is a promising strategy.
Error-prone PCR is a widely utilized technique in directed evolution. By altering the reaction conditions, it increases the mutation rate during PCR, leading to the random incorporation of incorrect bases into the amplified genes at a certain frequency, thereby generating a population of randomly mutated DNA. Among these mutants, some may exhibit improved performance. Our objective is to carry out directional evolution based on the existing high-activity sequences and obtain sequences with higher enzyme activity. We employed error-prone PCR for the directed evolution of these genes, followed by the expression of alginate lyases in Escherichia coli. The produced enzyme solution will then be reacted with alginate. We measured the enzymatic activity of each mutant, with the aim of identifying mutants with enhanced activity that hold potential for industrial application. Additionally, from the point of view of computational simulation, the possibility of obtaining high activity enzyme was discussed. We found a positive mutant protein molecule R30W. +
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+ Alginate, a polysaccharide found in brown algae, plays a role of great importance for the world both in marine ecosystems and in industrial applications. Nevertheless, the true potential of marine polysaccharides is limited in a way due to its disorganized branching and macromolecule figure, which leads to its low solubility and high solution viscosity. Besides, its capability to be easily absorbed by the body is weakened to a certain extent, leading to inconvenience to put it into further use, such as systemic therapies. The need to find its replacement is then highlighted. It’s noticed that with the glycosidic bonds between the β-D-mannuronic acid(M) and α-L-guluronic acid(G) residues cleaved away from alginate, a better material referred to as alginate oligosaccharide(AOS) is generated[1]. Studies have shown its anti-tumor, anti-virus, and anti-inflammatory effects. Moreover, easier diffusion and absorption features are shown on it as a result of its smaller size. It also functions in biological activities like signaling and biofilms penetration[2,3]. To make AOS available, the enzyme that specifically helps with the breakdown of alginate is necessary. Performing such unique ability to degrade alginate, alginate lyase deserves further improvement to become more efficient when it comes to facilitate the process. Thus, we planned to improve the enzyme activity of alginate lyase, through which we found the error-prone PCR method was possibly to achieve our goal.
Error-prone PCR is an evolution of standard PCR technology. It is a technique that makes DNA more prone to mismatches during the amplification process, hence it is also known as mismatch PCR or error-prone PCR. Error-prone PCR typically utilizes low-fidelity Taq DNA polymerase and alters some components of the PCR reaction system to reduce the fidelity of DNA replication during the PCR process, increasing the mutation rate and thus obtaining different DNA sequences or genes [4,5].

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+ My name is Kairong Cheng. I am an undergraduate from Ocean University of China. + +
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My name is Kairong Cheng. I am an undergraduate from Ocean University of China. I am an outgoing person and love to communicate with people. What I enjoy very much is reading and hiking. Life is the most precious thing we possess, which I want to use to do something meaningful. My motto is a quote from the philosopher Zhu Xi of the Song Dynasty: "It is unreasonable for a person to eat in this world without doing something."

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+ Education: Ocean University of China
undergraduate, major in Biology Science + +
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Education: Ocean University of China

undergraduate, major in Biology Science

Experience: 2024 Qingdao Marathon volunteer

Skill: Piano playing, Sketch drawing

Hobby: ski & skate & musical

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+ I'm Gu Yufei of OUC_DE, Ocean University of China, passionate about expanding my expertise through iDEC.  + +
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I'm Gu Yufei of OUC_DE, Ocean University of China, passionate about expanding my expertise through iDEC. I'm excited to engage with global peers, absorbing innovative ideas and experimental methods. The competition offers a comprehensive learning experience, from devising plans to executing experiments, analyzing data, and presenting findings. This hands-on approach will sharpen my skills and teamwork, equipping me with tools for future research and scientific contributions. I'm thrilled for the iDEC journey, ready to challenge and evolve both personally and academically.

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+ My name is Qiu Hui and I come from China. Doing research keeps me thinking, and I enjoy the process of thinking. + +
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My name is Qiu Hui and I come from China. Doing research keeps me thinking, and I enjoy the process of thinking.

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My name is Zhaorui(Elijah), Jiang. I am an undergraduate student at Ocean University of China & Heriot-Watt University, majored in Computer Science and Technology & Robotics. My research focuses on Robotics, bioinformatics and AI for Life Science — in particular,Graph Neural Network, Explainable Artificial Intelligence.

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OUC student majoring in biological science～

hobbies: photography, music, reading...

favorite writer: Hermann Hesse

favorite singer: Anpu

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+ Lu Zhennan from Ocean University of China + +
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Lu Zhennan from Ocean University of China

“Take baby steps!”

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+ This summer I was lucky to meet a group of lovely friends. + +
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This summer I was lucky to meet a group of lovely friends. We made great efforts to overcome a lot of difficulties in the experiment. I believe no matter what the result is, everyone has learned a lot.

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+ Role: Captain of the team. Responsible for biological experiments, including arranging experimental scheme and orgnizing discussions. + +
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Name: Yu Erjie

Gender: male

Role: Captain of the team. Responsible for biological experiments, including arranging experimental scheme and orgnizing discussions.

ENFP: INFJ

Hobbies：photography, playing badminton and ping pong, calligraphy

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At present, there have been many molecular modifications for alginate, mainly focused on site directed mutagenesis and domain recombination. For example, Lu et al. obtained a mutant with a 75.80% increase in enzyme activity compared to the wild type through site mutagenesis[8]. Zhang et al. obtained a mutant with enzyme activity 2.35 times higher than the wild-type through domain recombination[9]. However, the use of error prone PCR for the modification of alginate enzymes is still limited. Li et al. used error prone PCR technology to increase the activity of alginate, causing enzyme activity to be 2.41 times higher than before [10]. Our experiments have confirmed the significant potential of error prone PCR to modify alginate enzyme activity, which can be applied to improve alginate enzyme activity, increase alginate oligosaccharide production, and meet industrial needs.

Alginate oligosaccharides have extremely high value, and their main production method is still the degradation of alginate by alginate enzymes. Wild type enzymes often have low activity. However, there are still not many highly active alginate enzymes that have been artificially modified. This experiment is a beneficial attempt. We hope to use error prone PCR technology to modify and obtain more highly active alginate enzymes in the future.

In the experiment, we noticed some issues that need to be studied and improved. Alginate cannot self color and lacks the necessary identification markers for high-throughput screening. The traditional DNS method is slightly cumbersome, and the method we use to detect the amount of product using the value of OD235 is relatively simple. However, the value of OD235 is difficult to accurately quantify the product. It can only be used for comparison, indicating that the activity of the mutant is higher than that of the wild type. In addition, this method may be affected by some interfering factors. 

Due to the reaction characteristics, the electrophoretic bands of error-prone PCR products are not very bright, and sometimes there was not enough product which can be recovered. Our strategy is to conduct PCR reactions on multiple tubes simultaneously. 

During the dry lab, site-directed mutagenesis yielded the R30W variant, which demonstrated enhanced enzymatic activity relative to the 5ZU5 construct. This increase in activity may be attributed to the fact that, despite the molecular docking scores remaining invariant between R30W and 5ZU5, the number of binding sites with sodium alginate for R30W has been augmented. An increased number of binding sites could potentially amplify the intermolecular interactions between the protein and its ligand, culminating in a heightened binding affinity and, consequently, an elevation in the protein's bioactivity. 

We also encountered the issue of inconsistent standards for the activity of alginate enzymes. We attempt to construct a model that can predict the enzyme activity of a specific sequence encoding alginate enzymes. However, the inconsistent enzyme activity measurement standards in the papers have posed difficulties for our attempts to construct models. We hope to develop a unified and easily measurable standard to measure the activity of alginate enzymes.


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Reference

[1]Cheng D, Jiang C, Xu J, et al. Characteristics and applications of alginate lyases: A review[J]. International Journal of Biological Macromolecules, 2020, 164: 1304-1320. 

DOI：https://doi.org/10.1016/j.ijbiomac.2020.07.199

[2] A La Teng Zhu La, Hu YF. Advances in the preparation of alginate oligosaccharides and its biological functions. Chinese Journal of Biotechnology, 2022, 38(1): 104-118.

DOI: https://dx.doi.org/10.13345/j.cjb.210377

[3] HAN Yang, WANG Shujing.The anti-tumor effect of brown algae polysaccharide and its derivatives[J]. Chemistry of Life,2019(04):673-680.

DOI: https://dx.doi.org/10.13488/j.smhx.20180130

[4] Palackal N, Brennan Y, Callen W N, et al. An evolutionary route to xylanase process fitness[J]. Protein science, 2004, 13(2): 494-503. 

DOI：https://doi.org/10.1110/ps.03333504

[5] Wang Y, Fu Z, Huang H, et al. Improved thermal performance of Thermomyces lanuginosus GH11 xylanase by engineering of an N-terminal disulfide bridge[J]. Bioresource Technology, 2012, 112(5): 275–279. 

DOI：https://doi.org/10.1016/j.biortech.2012.02.092

[6] Zhang K, Liu T, Liu W, et al. Structural insights into the substrate-binding cleft of AlyF reveal the first long-chain alginate-binding mode[J]. Acta Crystallographica Section D: Structural Biology, 2021, 77(3): 336-346.

DOI：https://doi.org/10.1107/s205979832100005x

[7] Zhang Hongxiu, Liu Xiaohua, Liu Weizhi. Study on the New Alginate Lyase AlyPC1 from Marine Bacterium Pseudoalteromonas sp. 01[J].Periodical of Ocean University of China,2024,54(02):84-88+105. 

DOI：http://dx.doi.org/10.16441/j.cnki.hdxb.20220128

[8]Lu Y, Zhou J, Gu Q, et al. Cloning, expression and improvement of catalytic activity of alginate lyase by site-directed mutation[J]. Systems Microbiology and Biomanufacturing, 2022, 2(3): 555-567.

DOI：https://doi.org/10.1007/s43393-022-00084-w

[9]Zhang Z, Tang L, Bao M, et al. Functional characterization of carbohydrate-binding modules in a new alginate lyase, TsAly7B, from Thalassomonas sp. LD5[J]. Marine drugs, 2019, 18(1): 25. 

DOI：https://doi.org/10.3390/md18010025

[10] Li Shu,Zhang Wei,Zhao Chunmei.Directed Evolution of Alginate Lyase Alg-2 Based on Error Prone PCR[J].Food Science,2019(04):146-151.

DOI：http://dx.doi.org/10.7506/spkx1002-6630-20180207-100

[11] Qianqian Lyu, Keke Zhang, Qiaoyun Zhu, Zhijian Li, Yujie Liu, Elisabeth Fitzek, Tanner Yohe, Liming Zhao, Weihua Li, Tao Liu, Yanbin Yin, Weizhi Liu. Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes, Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1862, Issue 9, 2018, Pages 1862-1869, ISSN 0304-4165

DOI: https://doi.org/10.1016/j.bbagen.2018.05.024


Acknowledgment

Throughout the writing of this dissertation, we have received a great deal of support and assistance. We would first like to thank our supervisor, Prof. Weizhi Liu, whose expertise was invaluable in formulating the research questions and methodology.Your insightful feedback pushed us to sharpen our thinking and brought our work to a higher level.

We would especially like to thank our advisor, Junyi Huang, who provided meticulous assistance throughout the entire process of our experiment. Without his guidance, it would not have been possible for us to complete the experiment successfully.

We would particularly like to acknowledge all of our team members, for their wonderful collaborationand persistent efforts.

We would also like to express our gratitude to WeihaoZhou as well asother graduate studentsin the lab, who provided extremely valuable guidance on the operational details of this experiment, ensuring the progress of our work.

We are grateful to our classmates, the 2024 iGEM team, OUC_China for lending us important laboratory equipment.

Finally,we also would like to express our sincere gratitude to our college--College of Marine Life Sciences, Ocean University of Chinafor providing us with the venue and experimental reagents,and encouragingus to successfully complete ourresearch. We are grateful to Professor XianghongWang forhis efforts in supplementing the experimental materials.

Supplementary data.pdf

OUC_DE Author List_2024.pdf

Protocol—OUC_DE—Directed evolution of alginate lyase for enhanced-L.pdf

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1. Wet Lab

1.1 Plasmid and strain

We used E.coli BL21(DE3)(provided by our instructor's lab) as recipient and pET32a vector which contains an ampicillin resistance gene as the selection marker.

1.2 Extraction of pET32a-AlyAYO plasmid and double enzyme digestion

Inoculate 50 µL of glycerol bacteria(provided by our instructor's lab) into 5 mL of LB liquid medium(HB0128, hopebio) containing a one-thousandth concentration of ampicillin(Sangon biotech) and incubate overnight at 37℃ and 180rpm on a constant temperature shaker(MQL-61R, Shanghai Minquan Instrument Co., Ltd). The plasmid was extracted with a plasmid extraction kit (E.Z.N.A. Plasmid DNA Mini Kit Ⅰ, V spin, Omega Bio-Tek). The concentration and quality of the extracted plasmids were detected by Nano Drop (Thermo Scientific Nanodrop One).

Then we produced double enzyme digestion to collect pET32a linearized plasmid and AlyAYO gene. The reaction system was set as Table 1.

Table 1 Composition of Plasmid Extraction Reaction Mixture

Reagent Name

Dosage(μL)

plasmid

45

BamHⅠ

1.5

XhoⅠ

1.5

10× K Buffer

5.3

The reaction was performed at 30℃ for at least 6h. The product was examined by 1% agarose (1110GR100, Biofroxx ) gel electrophoresis and then recovered with gel extraction kit (E.Z.N.A. Gel Extraction Kit V spin, Omega Bio-Tek).

1.3 Error-prone PCR

The PCR primers were designed with the intention of introducing errors, using the following parameters: primer F of GGATCCATGGCGCAGCTGGACCCGA and an annealing temperature of 70.9℃; primer R of CTCGAGTTAGTGTTTGATATCCAGCTGGTAGAAGCTAACCTGG and annealing temperature of 65.9℃. The error-prone PCR was carried out using Error-prone PCR kit (Controlled Error-prone PCR Kit (ZY-160903), Zebra Bio), the template was the extracted plasmid, and the two mutation numbers of 5,8 were selected and 35 cycles were carried out for 4 times.

The reaction systems with AlyAYO template concentrations of 1ng/μL and 10ng/μL were set as Table 2.

Table 2 Composition of Error-prone PCR Reaction Mixture

expected number of mutations per 1000bp

5

8

5× Mix

6μl

6μl

MnCl2

4μl

4μl

dGTP

1μl

4μl

template

1μl

1μl

pF

1μl

1μl

pR

1μl

1μl

DNA polymerase

0.5μl

0.5μl

ddH2O

15.5μl

12.5μl


After pre-denaturation at 94℃ for 3min, 35 cycles of reaction were performed: denaturation at 94℃for 1 min, annealing at 60.9℃ for 1 min and extension at 72℃ for 3min(A300 Fast Thermal Cycler，LongGene). The PCR products were examined by electrophoresis on 1% agarose gel.

1.4 Double digestion and agarose gel electrophoresis for product recovery

Cycle-pure Kit (E.Z.N.A. Cycle-pure Kit(D6492-02), Omega Bio-Tek) was then used to recover the mutated AlyAYO gene from the product of error-prone PCR. Then the mutated genes were subjected to digestion with two enzymes(BamHⅠ(1010S) and XhoⅠ(1094S), Takara) and K Buffer(Takara, comes with BamHⅠ enzyme). Add 1.5μl of each enzyme, and the amount of K Buffer added is one tenth of the total system. Agarose gel electrophoresis was then performed to recover the mutated AlyAYO gene using an agarose gel recovery kit (E.Z.N.A. Gel Extraction Kit V spin, Omega Bio-Tek). The digested products were incubated at 30°C for at least 6 hours. The concentration and quality of the recovered products were subsequently determined using a Nano Drop spectrophotometer (Thermo Scientific NanoDrop one).

1.5 Connections and conversions

The mutant gene and pET32a plasmid which had been digested into a linear form by two enzyme should be connected together.

The connecting reaction system was set as Table 3.

Table 3 Composition of Connecting Reaction Mixture

Reagent Name

Dosage(μL)

gene

7

vector

1

T4 DNA Ligase (2011A, Takara)

1

T4 DNA Ligase Buffer (Takara, comes with T4 DNA Ligase)

1


The ligation process should be carried out for a minimum of four hours at 16°C.

The ligation product should be added to the receptor cell, and the volume of the ligation product should not exceed 1/10 of the receptor cell. The mixture should be gently agitated, incubated on ice for 30 minutes, and then heated to 42°C for 90 seconds without agitation. Subsequently, the mixture was immediately transferred to an ice water bath for 2-3 minutes, after which 900 μL of Amp-free LB medium was added. The bacteria were then incubated in a constant temperature shaker with oscillation at 37°C and 150 rpm for 45 minutes. A 45-minute incubation period is required for the bacterium to revive and for the resistance gene to be expressed. Centrifugation at 2500 g for 5 minutes is then performed, after which the supernatant of 900μL is aspirated. The bacterium is then resuspended in the remaining medium and spread uniformly on the resistance plate with a sterile applicator stick. Once the bacterial liquid has been absorbed by the plate, it is incubated inverted at 37°C overnight. At the same time, the unmutated wild-type bacterial fluid is used to delineate the control group.

1.6 96-well plate culture and induction

A volume of 150μl of Amp-containing LB medium should be added to each well of a 96-well plate(96-well Clear Flat Bottom UV-Transparent Microplate, corning). The colonies should then be picked from the plate and transferred into the wells, where they should be incubated at 37°C 180 rpm with oscillation until the true absorbance of the bacterial solution reaches 0.6-0.8. The true absorbance is defined as follows: true absorbance = (measured absorbance – blank absorbance) x 1.3125. Because the optical path length of our enzyme-linked immunosorbent assay (ELISA) reader is different from the one used in the paper we referenced. Before induction, we take 25μL of bacterial solution from each well and transfer it to another 96-well plate. After continuing to culture for several hours, we add an equal volume of 30% glycerol(10010618, Shanghai Hushi Laboratory Equipment Co., Ltd) for seed preservation. The remaining bacterial solution should then be supplemented with the appropriate amount of IPTG(Sangon Biotech) to achieve the desired working concentration（0.2mmol/L）. The culture was incubated in a constant temperature shaker set at 16°C with an agitation speed of 180 rpm for a period of 18 to 20 hours.[6,7]

1.7 Detection of enzyme activity

The bacterial precipitate should be obtained by centrifuging the 96-well plate at 4000 rpm. A volume of 150μl of bacterial lysate should be added to each well, after which the plate should be incubated at 37°C in a constant temperature incubator for one hour. Subsequently, 190μl of substrate solution should be added to the UV 96-well plate, and the contents should be suctioned. The substrate solution contains 0.2% sodium alginate(Shanghai Yuanye Bio-Technology Co., Ltd), 50mM Tris HCl(self-made by Tris and HCl, Tris was from Biofroxx, 1115GR500) solution with pH 7.5, and 200mM NaCl(10019318, Shanghai Hushi Laboratory Equipment Co., Ltd). A volume of 10μl of the diluted enzyme solution (enzyme solution: diluted buffer = 2:3, the composition of the diluted buffer is the same as the substrate solution but does not contain sodium alginate) should be added to the substrate solution with a row gun. The solution should be mixed gently to prevent the formation of bubbles and then the Bio-Tek Epoch Microplate Spectrophotometer should be used to determine the 235 nm wavelength absorbance.

2. Dry Lab

2.1 Protein obtaining, imitating, docking and analyzing

First, we obtained the 5ZU5 protein sequence from PDB[11], which was later analyzed in detail. Using BLAST(Basic Local Alignment Search Tool) on the National Center for Biotechnology Information website, protein sequences that shared no less than 90% similarities with 5ZU5 protein sequence were selected. Respectively, Consensus Finder and CB-Dock helped us with analyzing several highly conserved sites and identifying the binding sites where proteins and alginate interact. We then performed site-directed mutagenesis on those regions. We used Alphafold 3 to generate the structure of mutant proteins, performed molecular docking and analyzed the results. Since CB-Dock uses blind docking as its protein docking strategy, which led to the possibility of substrates binding to different regions, we calculated the potential substrate pocket area to ensure that substrates and enzymes bound at the correct sites. Additionally, the binding affinity of certain protein docking interactions was analyzed to determine whether it was acceptable.


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1.Wet Lab

1.1 error-prone PCR 

The alginate gene we modified was AlyAYO, with a total length of 930bp. We cultured E. coli BL21 containing pET32a-AlyAYO plasmids from its glycerol stock which is from Marine Enzyme Laboratory of Ocean University of China and extracted pET32a-AlyAYO plasmids. Then, we digested pET32a-AlyAYO plasmids with BamHⅠand XhoⅠ to collect pET32a plasmid and AlyAYO gene, which were expression vector and the template of error-prone PCR.

Controlled error-prone PCR Kit (No. ZY-160903) was used to preform sequential error-prone PCR on AlyAYO. The set of number of cycles was 35. The expected mutation values are set to 5 per 1000bp and 8 per 1000bp. In each tube, 5μL of 30μl product was used for agarose gel electrophoresis. The results of error-prone PCR products after agarose gel electrophoresis are shown in Fig1.

Fig1 Product electrophoresis results

M: Marker2000

1: Error-prone PCR products with a concentration of 10ng/μL as template and the expected mutation value is set to 5 per 1000bp

2: Error-prone PCR products with a concentration of 1ng/μL as template and the expected mutation value is set to 5 per 1000bp

3: Error-prone PCR products with a concentration of 10ng/μL as template and the expected mutation value is set to 8 per 1000bp

4: Error-prone PCR products with a concentration of 1ng/μL as template and the expected mutation value is set to 8 per 1000bp

1.2 Construction of expression vector

The remaining product was digested sequentially with BamHⅠand XhoⅠ. Then we ligated error-prone PCR product into the corresponding sites of the pET32a plasmid to construct the vector and the vector was transformed into E. coli BL21 which was self-made by Marine Enzyme Laboratory of Ocean University of China. 

1.3 Enzymatic activity analysis of expressed proteins

We picked single colonies which are successfully transformed and cultured them in 96 well plates. After induction with IPTG, we lysed the cells, used the supernatant as the crude enzyme solution, and measured the enzyme activity. 

One unit of enzyme activity was defined as an increase of 1 OD235 unit per min. The enzyme activity of original strain was 12.350U/ml. Among the 32 mutant strain, the enzyme activity of some of them have significantly increased, which are shown as follows. The enzyme activity of the mutant with the highest activity is more than three times that of the wild type. 

Fig2 The enzyme activity of original strain and its mutant strains.


2. Dry Lab

2.1 A positively mutant protein R30W

Finally, we obtained a positively mutant protein R30Wwhose amino acid sequence is GPPDLGTDDDDKAMADIASDFPNNKETGEALLTPVDATASSHDGNGPDWLIDQDLTTRWSSAGDGEWAMLDYGSVQEFDAVQASFSKGNERQSKFDIQVSVDGETWTTVLENQLSSGKAIGLERFQFEPAVKARYVRYVGHGNTKNGWNSVTGLAAVNCSINACPASQIITSDVVAAEAVLIAEMKAAEKARKAARKDLRSGNFGVAAVYPCETSVKCDTRSALPVPTGLPATPVAGNAPSENFDMTHWYLSQPFDHDKNGKPDDVSEWNLANGYQHPEIFYTADDGGLVFKSYVKGVRTSKNTKYARTELREMMRRGDQSISTKGVNKNNWVFSSAPEADLEAAAGIDGVLEATLKIDHATTTGNANEVGRFIIGQIHDQNDEPIRLYYRKLPNQPTGAVYFAHESQDATKEDFYPLVGDMTAEVGEDGIALGEVFSYRIDVKGNTMTVTLMREGKDDVVQVVDMSNSGYDVGGKYMYFKAGVYNQNISGDLDDYSQATFYQLDVSHDQYKK. Compared with 5ZU5, the docking score of R30W has not changed, but the number of binding sites with sodium alginate has increased from 25 to 37. More binding sites may enhance the interaction between protein and ligand, resulting in enhanced binding affinity, thereby improving the biological activity of the protein. The 3D docking molecule structure of the R30W is shown in Figure 3.

Fig3The 3D docking molecule structure of the R30W.

The amino acids marked in purple in the figure are the amino acids that bind to the substrate, which are ASP36, ALA37, THR38, ALA39, HIS42, ASP43, GLY44, ASN45, GLY46, PRO47, ASP48, TRP49, LYS305, TYR306, THR363, ALA367, ASN368, GLU369, VAL370, ARG372, ILE374, ARG387, TYR389, ARG391, LEU393, PRO394, ASN395, GLN396, TYR402, ALA404, GLU413, PHE415, MET422, THR423, GLU425, TYR485, GLN487.


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+ Alginate oligosaccharides have found extensive applications in the fields of food, healthcare, and biomedicine. Alginate lyase serves as the primary tool for the preparation of alginate oligosaccharides. Thus, the identification of alginate lyases with high enzymatic activity is of significant importance. However, the activity of wild-type alginate lyases is often insufficient for practical applications. Therefore, engineering alginate lyases at the molecular level to enhance their activity is a promising strategy.

Error-prone PCR is a widely utilized technique in directed evolution. By altering the reaction conditions, it increases the mutation rate during PCR, leading to the random incorporation of incorrect bases into the amplified genes at a certain frequency, thereby generating a population of randomly mutated DNA. Among these mutants, some may exhibit improved performance. Our objective is to carry out directional evolution based on the existing high-activity sequences and obtain sequences with higher enzyme activity. We employed error-prone PCR for the directed evolution of these genes, followed by the expression of alginate lyases in Escherichia coli. The produced enzyme solution will then be reacted with alginate. We measured the enzymatic activity of each mutant, with the aim of identifying mutants with enhanced activity that hold potential for industrial application. Additionally, from the point of view of computational simulation, the possibility of obtaining high activity enzyme was discussed. We found a positive mutant protein molecule R30W. +
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+ Key words +
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+ directed evolution +
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+ alginate +
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+ error-prone PCR +
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+ Alginate, a polysaccharide found in brown algae, plays a role of great importance for the world both in marine ecosystems and in industrial applications. Nevertheless, the true potential of marine polysaccharides is limited in a way due to its disorganized branching and macromolecule figure, which leads to its low solubility and high solution viscosity. Besides, its capability to be easily absorbed by the body is weakened to a certain extent, leading to inconvenience to put it into further use, such as systemic therapies. The need to find its replacement is then highlighted. It’s noticed that with the glycosidic bonds between the β-D-mannuronic acid(M) and α-L-guluronic acid(G) residues cleaved away from alginate, a better material referred to as alginate oligosaccharide(AOS) is generated[1]. Studies have shown its anti-tumor, anti-virus, and anti-inflammatory effects. Moreover, easier diffusion and absorption features are shown on it as a result of its smaller size. It also functions in biological activities like signaling and biofilms penetration[2,3]. To make AOS available, the enzyme that specifically helps with the breakdown of alginate is necessary. Performing such unique ability to degrade alginate, alginate lyase deserves further improvement to become more efficient when it comes to facilitate the process. Thus, we planned to improve the enzyme activity of alginate lyase, through which we found the error-prone PCR method was possibly to achieve our goal.
Error-prone PCR is an evolution of standard PCR technology. It is a technique that makes DNA more prone to mismatches during the amplification process, hence it is also known as mismatch PCR or error-prone PCR. Error-prone PCR typically utilizes low-fidelity Taq DNA polymerase and alters some components of the PCR reaction system to reduce the fidelity of DNA replication during the PCR process, increasing the mutation rate and thus obtaining different DNA sequences or genes [4,5].

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+ Kairong Cheng +
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+ My name is Kairong Cheng. I am an undergraduate from Ocean University of China. + +
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+

My name is Kairong Cheng. I am an undergraduate from Ocean University of China. I am an outgoing person and love to communicate with people. What I enjoy very much is reading and hiking. Life is the most precious thing we possess, which I want to use to do something meaningful. My motto is a quote from the philosopher Zhu Xi of the Song Dynasty: "It is unreasonable for a person to eat in this world without doing something."

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+ Jialin Cheng +
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+ Education: Ocean University of China
undergraduate, major in Biology Science + +
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Education: Ocean University of China

undergraduate, major in Biology Science

Experience: 2024 Qingdao Marathon volunteer

Skill: Piano playing, Sketch drawing

Hobby: ski & skate & musical

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+ I'm Gu Yufei of OUC_DE, Ocean University of China, passionate about expanding my expertise through iDEC.  + +
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I'm Gu Yufei of OUC_DE, Ocean University of China, passionate about expanding my expertise through iDEC. I'm excited to engage with global peers, absorbing innovative ideas and experimental methods. The competition offers a comprehensive learning experience, from devising plans to executing experiments, analyzing data, and presenting findings. This hands-on approach will sharpen my skills and teamwork, equipping me with tools for future research and scientific contributions. I'm thrilled for the iDEC journey, ready to challenge and evolve both personally and academically.

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+ + + + + + + + + + + + + + diff --git a/mobile/goods/2656213/index.html b/mobile/goods/2656213/index.html new file mode 100644 index 0000000..478bd26 --- /dev/null +++ b/mobile/goods/2656213/index.html @@ -0,0 +1,2075 @@ + + + + + Hui Qiu + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + +
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+ Hui Qiu +
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+ My name is Qiu Hui and I come from China. Doing research keeps me thinking, and I enjoy the process of thinking. + +
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My name is Qiu Hui and I come from China. Doing research keeps me thinking, and I enjoy the process of thinking.

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+ Previous : + + Zhaorui Jiang + +
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+ Zhaorui Jiang +
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+ My name is Zhaorui(Elijah), Jiang. I am an undergraduate student at Ocean University of China & Heriot-Watt University,  + +
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My name is Zhaorui(Elijah), Jiang. I am an undergraduate student at Ocean University of China & Heriot-Watt University, majored in Computer Science and Technology & Robotics. My research focuses on Robotics, bioinformatics and AI for Life Science — in particular,Graph Neural Network, Explainable Artificial Intelligence.

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+ Yiqing Lu +
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+ OUC student majoring in biological science～ + +
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OUC student majoring in biological science～

hobbies: photography, music, reading...

favorite writer: Hermann Hesse

favorite singer: Anpu

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+ Previous : + + Zhennan Lu + +
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+ Lu Zhennan from Ocean University of China + +
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Lu Zhennan from Ocean University of China

“Take baby steps!”

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+ Yuting Zhan +
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+ This summer I was lucky to meet a group of lovely friends. + +
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This summer I was lucky to meet a group of lovely friends. We made great efforts to overcome a lot of difficulties in the experiment. I believe no matter what the result is, everyone has learned a lot.

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+ Role: Captain of the team. Responsible for biological experiments, including arranging experimental scheme and orgnizing discussions. + +
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Name: Yu Erjie

Gender: male

Role: Captain of the team. Responsible for biological experiments, including arranging experimental scheme and orgnizing discussions.

ENFP: INFJ

Hobbies：photography, playing badminton and ping pong, calligraphy

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