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<!DOCTYPE html>
<html lang="en">
<head>
<meta charset="UTF-8">
<title>Description</title>
<meta name="viewport" content="width=device-width, initial-scale=1, user-scalable=no">
<script src="js/jquery.js"></script>
<link rel="stylesheet" href="css/bootstrap.min.css">
<script src="js/bootstrap.min.js"></script>
<link rel="stylesheet" href="css/general.css">
<script src="js/general.js"></script>
<link rel="stylesheet" href="css/article.css">
</head>
<body>
<nav id="nav-bar" class="navbar navbar-expand-lg navbar-light sticky-top"></nav>
<div id="title" class="col-12" style='-o-background-image: url("https://2021.igem.org/wiki/images/7/72/T--DUT_China--t_description.png");
-moz-background-image: url("https://2021.igem.org/wiki/images/7/72/T--DUT_China--t_description.png");
-webkit-background-image: url("https://2021.igem.org/wiki/images/7/72/T--DUT_China--t_description.png");
background-image: url("https://2021.igem.org/wiki/images/7/72/T--DUT_China--t_description.png");'>
<div>Description</div>
</div>
<section id="main-text">
<article class="article">
<h1>Description</h1>
<p>Wide spreading and utilization of plastic polyethylene terephthalate (PET) in the world has caused a large
quantity of environmental challenges and gained much attention. Because of its nonbiodegradability, a large
amount of plastic waste accumulation forms a global environmental crisis [1]. Notably, in 2016, Yoshida et
al. reported the discovery of the bacterium, <i>Ideonella sakaiensis</i> [2]. Microbe <i>Ideonella
sakaiensis</i> was reported to be capable of secreting two efficient enzymes to deconstruct PET polymers
in mild temperature. First, <i>Ideonella sakaiensis</i> PETase, a structurally well-characterized consensus
α/β-hydrolase fold enzyme, converts PET to mono-(2-hydroxyethyl) terephthalate (MHET). MHETase, the second
key enzyme, hydrolyzes MHET to the PET educts terephthalate and ethylene glycol [3].</p>
<p>However, this two-enzyme system degradation capacity is highly limited by inhibition effects, diffusion of
intermediates and PET surface physicochemical properties [4]. Here, we design a delicate multicomplex enzyme
system, in which short peptide tags (RIAD and RIDD) are applied to create scaffold-free modular enzymes
assemblies [5]. In order to effectively degrade microplastic PET particles, we construct enzymes of <i>Is</i>PETase
and MHETase and protein hydrophobin in our complex system via scaffold modular part, which reveal higher
catalytic efficiency in mild temperature. All proteins involved have unique functions in our system.
<i>Is</i>PETase and MHETase are two enzymes involved deconstructing polymer PET plastic to MHET and MHET to TPA
molecules, respectively. And hydrophobin protein, a small fungal protein, possess positive effects on
altering the physicochemical properties of PET surfaces and enzyme aggregation enhancement when it was fused
with PET degradation enzyme cutinase [6]. In conclusion, our work presents an innovative strategy to improve
PET degradation via biosynthetic factories and artificially designed proteins system that do not exist in
the nature.</p>
</article>
<article class="article ref">
<h1>References</h1>
<p>[1] Hachisuka Shin-ichi, Nishii Tarou, Yoshida Shosuke, & Cann Isaac. Development of a Targeted Gene
Disruption System in the Poly(Ethylene Terephthalate)-Degrading Bacterium Ideonella sakaiensis and Its
Applications to PETase and MHETase Genes. <i>Applied and Environmental Microbiology</i> 87, e00020-21.</p>
<p>[2] Yoshida S, Hiraga K, Takehana T, et al. A bacterium that degrades and assimilates poly(ethylene
terephthalate).[J]. <i>Science</i> 351, 1196-1199. (2016).</p>
<p>[3] Palm, G. J., Reisky, L., Böttcher, D. et al. Structure of the plastic-degrading Ideonella sakaiensis
MHETase bound to a substrate. <i>Nature Communications</i> 10, 1717 (2019).</p>
<p>[4] Knott, B. C. et al. Characterization and engineering of a two-enzyme system for plastics
depolymerization. <i>Proc Natl Acad Sci USA</i> 117, 25476–25485 (2020).</p>
<p>[5] Kang, W. et al. Modular enzyme assembly for enhanced cascade biocatalysis and metabolic flux. <i>Nature
Communications</i> 10, 4248 (2019).</p>
<p>[6] Ribitsch Doris et al. Enhanced Cutinase-Catalyzed Hydrolysis of Polyethylene Terephthalate by Covalent
Fusion to Hydrophobins. <i>Applied and Environmental Microbiology</i> 81, 3586–3592 (2015).</p>
</article>
</section>
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