A new catalytic activity of α-glycerolphosphate dehydrogenase: The enzymatic hydrolysis of p-nitrophenyl acetate

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

Frontiers in Bioengineering and Biotechnology ◽

10.3389/fbioe.2021.762854 ◽

2021 ◽

Vol 9 ◽

Author(s):

Rui Xue ◽

Yinping Chen ◽

Huan Rong ◽

Ren Wei ◽

Zhongli Cui ◽

...

Keyword(s):

Catalytic Activity ◽

Enzymatic Hydrolysis ◽

Polyethylene Terephthalate ◽

Binding Domain ◽

Plastic Pollution ◽

Pet Waste ◽

Chitin Binding Domain ◽

C Terminus ◽

Measurable Activity ◽

Hydrolysis Of

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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