Enhanced Degradation of Insoluble Chitin: Engineering High-Efficiency Chitinase Fusion Enzymes for Sustainable Applications
SSRN, ISSN: 1556-5068
2024
- 18Usage
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
N-acetyl-D-glucosamine (GlcNAc) and its dimer (GlcNAc)2 are degradation products of chitin waste with great potential in therapeutic and agricultural applications. However, the hydrolysis of insoluble chitin by chitinases remains a major bottleneck. This study investigated the biochemical properties and catalytic mechanisms of PoChi chitinase obtained from Penicillium oxalicum with a focus on enhancing its efficiency during the degradation of insoluble chitin. Recombinant plasmids were engineered to incorporate chitin-binding (ChBD) and/or fibronectin III (FnIII) domains. Notably, PoChi-FnIII-ChBD exhibited the highest substrate affinity (Km = 2.675 mg/mL) and a specific activity of 15.44 U/mg, which surpass those of previously reported chitinases. Our findings propose a novel strategy for the optimization of chitinases, paving the way for industrial biotechnology applications that advance environmental sustainability and efficient utilization of chitinous waste.
Bibliographic Details
Elsevier BV
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