期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 108, 期 -, 页码 893-901出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2017.10.182
关键词
Protein engineering; Enzyme; Biocatalysis; Chemically modified enzyme; Catalytic activity; Rational design; Directed evolution
Over the past years, technological and scientific advances have proven biocatalysis as a sustainable alternative than traditional chemical catalysis including organo- or metallocatalysis. In this context, immobilization based approaches represent simple but effective routes for engineering enzyme catalysts with higher activities than wild-type derivatives. Many enzymes including oxidoreductases have been engineered by rational and directed evolution, to realize the catalytic activity, enantioselectivity, and stability attributes which are essential for their biotechnological exploitation. Induce yet stable activity in enzyme catalysis offer new insights and motivation to engineer efficient catalysts for practical and commercial purposes. It has now become possible to envisage substrate accessibility to the catalytic site of the enzyme by current computational capabilities that reduce the experimental work related to the enzyme selection, screening, and engineering. Herein, state-of-the-art protein engineering approaches for improving enzymatic activities including chemical modification, directed evolution, and rational design or their combination methods are discussed. The emphasis is also given to the applications of the resulting tailored catalysts ranging from fine chemicals to novel pharmaceutical compounds that use biocatalysts as a vital step. (C) 2017 Elsevier B.V. All rights reserved.
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