Data-driven strategies for the computational design of enzyme thermal stability: trends, perspectives, and prospects

Bibliographic Details
Title: Data-driven strategies for the computational design of enzyme thermal stability: trends, perspectives, and prospects
Authors: Dou Zhixin, Sun Yuqing, Jiang Xukai, Wu Xiuyun, Li Yingjie, Gong Bin, Wang Lushan
Source: Acta Biochimica et Biophysica Sinica, Vol 55, Pp 343-355 (2023)
Publisher Information: China Science Publishing & Media Ltd., 2023.
Publication Year: 2023
Collection: LCC:Biochemistry
LCC:Genetics
Subject Terms: enzyme design, data-driven, machine learning, thermal stability, Biochemistry, QD415-436, Genetics, QH426-470
More Details: Thermal stability is one of the most important properties of enzymes, which sustains life and determines the potential for the industrial application of biocatalysts. Although traditional methods such as directed evolution and classical rational design contribute greatly to this field, the enormous sequence space of proteins implies costly and arduous experiments. The developm ent of enzyme engineering focuses on automated and efficient strategies because of the breakthrough of high-throughput DNA sequencing and machine learning models. In this review, we propose a data-driven architecture for enzyme thermostability engineering and summarize some widely adopted datasets, as well as machine learning-driven approaches for designing the thermal stability of enzymes. In addition, we present a series of existing challenges while applying machine learning in enzyme thermostability design, such as the data dilemma, model training, and use of the proposed models. Additionally, a few promising directions for enhancing the performance of the models are discussed. We anticipate that the efficient incorporation of machine learning can provide more insights and solutions for the design of enzyme thermostability in the coming years.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1672-9145
Relation: https://doaj.org/toc/1672-9145
DOI: 10.3724/abbs.2023033
Access URL: https://doaj.org/article/ac98722c075e4671a73846e40f266988
Accession Number: edsdoj.98722c075e4671a73846e40f266988
Database: Directory of Open Access Journals
More Details
ISSN:16729145
DOI:10.3724/abbs.2023033
Published in:Acta Biochimica et Biophysica Sinica
Language:English