Fusion of Chitin-Binding Domain From Chitinolyticbacter meiyuanensis SYBC-H1 to the Leaf-Branch Compost Cutinase for Enhanced PET Hydrolysis

Polyethylene terephthalate (PET) is a mass-produced petroleum-based non-biodegradable plastic that contributes to the global plastic pollution. Recently, biocatalytic degradation has emerged as a viable recycling approach for PET waste, especially with thermophilic polyester hydrolases such as a cutinase (LCC) isolated from a leaf-branch compost metagenome and its variants. To improve the enzymatic PET hydrolysis performance, we fused a chitin-binding domain (ChBD) from Chitinolyticbacter meiyuanensis SYBC-H1 to the C-terminus of the previously reported LCCICCG variant, demonstrating higher adsorption to PET substrates and, as a result, improved degradation performance by up to 19.6% compared to with its precursor enzyme without the binding module. For compare hydrolysis with different binding module, the catalytic activity of LCCICCG-ChBD, LCCICCG-CBM, LCCICCG-PBM and LCCICCG-HFB4 were further investigated with PET substrates of various crystallinity and it showed measurable activity on high crystalline PET with 40% crystallinity. These results indicated that fusing a polymer-binding module to LCCICCG is a promising method stimulating the enzymatic hydrolysis of PET.

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Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

Current Nanoscience ◽

10.2174/1573413714666180611081759 ◽

2019 ◽

Vol 15 (3) ◽

pp. 296-303 ◽

Cited By ~ 5

Author(s):

Swapnil Gaikwad ◽

Avinash P. Ingle ◽

Silvio Silverio da Silva ◽

Mahendra Rai

Keyword(s):

Catalytic Activity ◽

Enzymatic Hydrolysis ◽

Immobilized Enzyme ◽

Free Enzyme ◽

Magnetic Nanomaterials ◽

Sugar Production ◽

Cellulase Enzyme ◽

Enzymatic Hydrolysis Of Cellulose ◽

Hydrolysis Of Cellulose ◽

Hydrolysis Of

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.

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Substrate Factors that Influence Cellulase Accessibility and Catalytic Activity During the Enzymatic Hydrolysis of Lignocellulosic Biomass

Fungal Cellulolytic Enzymes ◽

10.1007/978-981-13-0749-2_13 ◽

2018 ◽

pp. 239-256 ◽

Cited By ~ 1

Author(s):

Jinguang Hu ◽

Rui Zhai ◽

Dong Tian ◽

Jack N. Saddler

Keyword(s):

Catalytic Activity ◽

Enzymatic Hydrolysis ◽

Lignocellulosic Biomass ◽

Hydrolysis Of

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Turbidimetric analysis of the enzymatic hydrolysis of polyethylene terephthalate nanoparticles

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/j.molcatb.2013.08.010 ◽

2014 ◽

Vol 103 ◽

pp. 72-78 ◽

Cited By ~ 21

Author(s):

Ren Wei ◽

Thorsten Oeser ◽

Markus Barth ◽

Nancy Weigl ◽

Anja Lübs ◽

...

Keyword(s):

Enzymatic Hydrolysis ◽

Polyethylene Terephthalate ◽

Turbidimetric Analysis ◽

Hydrolysis Of

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A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch

FEBS Letters ◽

10.1016/j.febslet.2014.02.050 ◽

2014 ◽

Vol 588 (7) ◽

pp. 1161-1167 ◽

Cited By ~ 27

Author(s):

Hui Peng ◽

Yunyun Zheng ◽

Maojiao Chen ◽

Ying Wang ◽

Yazhong Xiao ◽

...

Keyword(s):

Enzymatic Hydrolysis ◽

Soluble Starch ◽

Binding Domain ◽

Carbohydrate Binding ◽

New Family ◽

Carbohydrate Binding Modules ◽

Hydrolysis Of

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Expression and Characterization of the Chitin-Binding Domain of Chitinase A1 from Bacillus circulans WL-12

Journal of Bacteriology ◽

10.1128/jb.182.11.3045-3054.2000 ◽

2000 ◽

Vol 182 (11) ◽

pp. 3045-3054 ◽

Cited By ~ 113

Author(s):

Masayuki Hashimoto ◽

Takahisa Ikegami ◽

Shizuka Seino ◽

Nobuhumi Ohuchi ◽

Harumi Fukada ◽

...

Keyword(s):

Hydrophobic Interactions ◽

Expression System ◽

Binding Activity ◽

Binding Domain ◽

Bacillus Circulans ◽

Titration Calorimetry ◽

Affinity Column ◽

Chitin Binding Domain ◽

Wide Range ◽

Hydrolysis Of

ABSTRACT Chitinase A1 from Bacillus circulans WL-12 comprises an N-terminal catalytic domain, two fibronectin type III-like domains, and a C-terminal chitin-binding domain (ChBD). In order to study the biochemical properties and structure of the ChBD, ChBDChiA1 was produced in Escherichia coliusing a pET expression system and purified by chitin affinity column chromatography. Purified ChBDChiA1 specifically bound to various forms of insoluble chitin but not to other polysaccharides, including chitosan, cellulose, and starch. Interaction of soluble chitinous substrates with ChBDChiA1 was not detected by means of nuclear magnetic resonance and isothermal titration calorimetry. In addition, the presence of soluble substrates did not interfere with the binding of ChBDChiA1 to regenerated chitin. These observations suggest that ChBDChiA1recognizes a structure which is present in insoluble or crystalline chitin but not in chito-oligosaccharides or in soluble derivatives of chitin. ChBDChiA1 exhibited binding activity over a wide range of pHs, and the binding activity was enhanced at pHs near its pI and by the presence of NaCl, suggesting that the binding of ChBDChiA1 is mediated mainly by hydrophobic interactions. Hydrolysis of β-chitin microcrystals by intact chitinase A1 and by a deletion derivative lacking the ChBD suggested that the ChBD is not absolutely required for hydrolysis of β-chitin microcrystals but greatly enhances the efficiency of degradation.

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Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor

Journal of Membrane Science ◽

10.1016/j.memsci.2015.07.030 ◽

2015 ◽

Vol 494 ◽

pp. 182-187 ◽

Cited By ~ 28

Author(s):

Markus Barth ◽

Ren Wei ◽

Thorsten Oeser ◽

Johannes Then ◽

Juliane Schmidt ◽

...

Keyword(s):

Enzymatic Hydrolysis ◽

Polyethylene Terephthalate ◽

Membrane Reactor ◽

Ultrafiltration Membrane ◽

Hydrolysis Of

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Preparation and characterization of waterborne alkyd-amino baking coatings based on waste polyethylene terephthalate

Royal Society Open Science ◽

10.1098/rsos.191447 ◽

2020 ◽

Vol 7 (1) ◽

pp. 191447

Author(s):

Xia Yun ◽

Yang Xin-yi ◽

Gong Dun-hong ◽

Ding Yong-bo ◽

Shen Liang

Keyword(s):

Polyethylene Terephthalate ◽

Chemical Resistance ◽

Alkali Resistance ◽

Formaldehyde Resin ◽

Melamine Formaldehyde ◽

Pet Waste ◽

Amino Resin ◽

Excellent Adhesion ◽

Hydrolysis Of

The recycling of polyethylene terephthalate (PET) is the most attractive method for PET waste management because it not only decreases the load on landfill space, but also provides opportunities for reducing the use of raw petrochemical products. Therefore, in this investigation, neopentyl glycol is used for alcoholysis of waste PET, and glycolyzed PET product was applied for preparation of the waterborne alkyd resin. Furthermore, the waterborne alkyd-amino baking coatings were prepared from the waterborne alkyd based on glycolyzed waste PET and melamine formaldehyde resin and applied on tinplate. The waterborne alkyd-amino resin films showed excellent adhesion, balanced hardness and flexibility, high gloss and outstanding chemical resistance except for alkali resistance owing to hydrolysis of ester bonds.

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