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BlueEve04 committed Oct 7, 2024
2 parents b344e42 + 914ed4a commit e30e2e4
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4 changes: 4 additions & 0 deletions css/card.css
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.card-text-2 {
position: absolute;
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left:280px;
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right:80px;
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5 changes: 5 additions & 0 deletions css/style.css
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font-family: 'Times New Roman', Times, serif;
top: 14%;
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left: 10%;
width: 80%;
font-size: 80px;
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left: 2%;
font-size: 120px;
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z-index: 9;
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44 changes: 44 additions & 0 deletions index.html
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</div>

<div class="titlebox">
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<h1 class="title" id="title">Complete bio-degradation of PBAT <br> via evolved hydrolases and construction of an engineered Pseudomonas putida KT2440 strain</h1>
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<h1 class="title" id="title">Lorem ipsum dolor elit. Officia, voluptatibus!</h1>
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</div>
<script>
const title = document.getElementById('title');
Expand Down Expand Up @@ -196,8 +200,15 @@ <h1 class="title" id="title">Complete bio-degradation of PBAT <br> via evolved h
<!-- 夹在头和尾之间 -->
<section class="second_part" style="position: relative;top: 1000px;">
<div class="WhatisPBAT" id="pbContainer">
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<h1>What is PBAT?</h1>
Poly (butylene adipate-co-terephthalate) (PBAT), a polymer synthesized from the monomers terephthalic acid (TPA), adipic acid (AA), and 1,4-butanediol (BDO), has garnered significant attention as a biocompatible and degradable polymeric material, exhibiting considerable potential for widespread application in the realm of agricultural film technology.
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<h1>PBAT introduction</h1>
Poly (butylene adipate-co-terephthalate) (PBAT), a polymer synthesized from the monomers terephthalic acid (TPA), adipic
acid (AA), and 1,4-butanediol (BDO), has garnered significant attention as a biocompatible and degradable polymeric
material, exhibiting considerable potential for widespread application in the realm of agricultural film technology.
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</div>
<script>
const pbContainer = document.getElementById('pbContainer');
Expand Down Expand Up @@ -300,6 +311,7 @@ <h1>What is PBAT?</h1>
<!-- 易错DNA部分 -->
<div class="DNA_line_container" id="box">
<div class="DNA_box1" id="DNABox1">
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<div><h1>Challenges</h1>
Firstly, the natural degradation rate of PBAT is extremely slow. After three months of natural degradation, it can only be degraded by about 2.3%. Secondly, the PBAT decomposition rates of existing PBAT-degrading enzymes in room temperature are generally low, restricting its utilization in the context of agricultural practices. Additionally, PBAT hydrolysis products can be toxic, adversely affecting microbial metabolism and efficient substrate assimilation.</div>
</div>
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We identified three distinct enzyme candidates for targeted evolutionary engineering, with the objective of developing highly efficient PBAT hydrolases that exhibit optimal catalytic activity under room temperature conditions. Furthermore, we also aim to obtain an engineering <em>Pseudomonas putida
</em> KT2440 strain capable of catabolizing of PBAT-derived degradation products.
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<div><h1>Development of PBAT hydrolases</h1>
We selected IsPETase, BsLipA, and Lipase1028 as the starting points for directed evolution and established three
mutation libraries using error-prone PCR and site-directed mutagenesis. Hydrolysis zone screening method was employed to
endow them with the ability to degrade PBAT.</div>
</div>
<div class="DNA_box2" id="DNABox2">
<div>
<h1>Development of engineered Pseudomonas putida KT2440 strain</h1>

The evolved PBAT hydrolases were transformed into Pseudomonas putida KT2440-tph, which had undergone adaptive laboratory
evolution to acquire the ability to utilize terephthalic acid (TPA) and 1,4-butanediol (BDO) as carbon sources. This
allowed the construction of a KT2440 strain with high PBAT degradation capacity and the ability to grow using its
degradation products.
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</div>
</div>

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</script>
</section>

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<h1 class="t1 aos-hover-zoom" data-aos="fade-up-left" data-aos-duration="1500ms"><strong>Development of a secretion pathway in <em> Bacillus subtilis</em></strong><br><br>
We first established an efficient secretion system within Bacillus subtilis. The signal peptide AprE was fused to the N-terminus of the enzymes to enable them to be effectively secreted out of the cells via the Sec pathway. The successfully constructed protein exocytosis pathway allows for intuitive hydrolysis zones screening of the mutation libraries.
</h1>
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endow them with the ability to degrade PBAT.</h1>
<h1 class="t3 aos-hover-zoom" data-aos="fade-up-left" data-aos-duration="1500ms"><strong>Development of an engineered <em>Pseudomonas putida</em> KT2440 strain</strong><br><br>The evolved PBAT hydrolases
were transformed into <em>Pseudomonas putida</em> KT2440-tph, which had undergone adaptive laboratory
=======
<h1 class="t1 aos-hover-zoom" data-aos="fade-up-left" data-aos-duration="1500ms">Poly (butylene
adipate-co-terephthalate) (PBAT), a polymer synthesized from the monomers terephthalic acid (TPA),
adipic
acid (AA), and 1,4-butanediol (BDO), has garnered significant attention as a biocompatible and
degradable polymeric
material, exhibiting considerable potential for widespread application in the realm of agricultural film
technology.</h1>
<h1 class="t2 aos-hover-zoom" data-aos="fade-up-right" data-aos-duration="1500ms">We selected IsPETase,
BsLipA, and Lipase1028 as the starting points for directed evolution and established three
mutation libraries using error-prone PCR and site-directed mutagenesis. Hydrolysis zone screening method
was employed to
endow them with the ability to degrade PBAT.</h1>
<h1 class="t3 aos-hover-zoom" data-aos="fade-up-left" data-aos-duration="1500ms">The evolved PBAT hydrolases
were transformed into Pseudomonas putida KT2440-tph, which had undergone adaptive laboratory
>>>>>>> 914ed4aa4dc10d7c1a2a0c39d938781f31bfb64e
evolution to acquire the ability to utilize terephthalic acid (TPA) and 1,4-butanediol (BDO) as carbon
sources. This
allowed the construction of a KT2440 strain with high PBAT degradation capacity and the ability to grow
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