Design Strategy of PepNzymes-SH for an Emerging Catalyst with Serine Hydrolase-Like Functionality
Source abstract
Abstract
Serine hydrolases, as a class of green catalysts with hydrolytic and dehydrating activities, hold significant application value in the fields of biosynthesis and organic synthesis. However, practical applications face numerous challenges, including maintaining enzyme stability and managing usage costs. PepNzymes-SH, an emerging green catalytic material with enzyme-like activity, overcomes the operational limitations of natural enzymes and holds great promise as a substitute for hydrolases. Unfortunately, a systematic review of the design strategies for PepNzymes-SH is currently lacking. The core significance of this report lies in providing researchers with a comprehensive understanding and theoretical guidance through the summarization and performance evaluation of different design strategies of PepNzymes-SH. This review summarizes strategies for simulating and enhancing the stability of serine hydrolase active sites, oxyanion holes, and hydrophobic environmental structures. By comparing their catalytic activities, we assess the performance changes brought about by different strategies. Furthermore, the applications of PepNzymes-SH in the chemical, biomedicine, and environmental fields are also discussed.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Supramolecular Self-Assembly in Materials · MXene and MAX Phase Materials
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology
Chinese Academy of Sciences
Shandong Energy Institute
Qingdao New Energy Shandong Laboratory
University of Chinese Academy of Sciences
Funding
Taishan Scholar Project of Shandong Province
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