Significant Improvement of Both Catalytic Efficiency and Stability of Fructosyltransferase from Aspergillus niger by Structure-Guided Engineering of Key Residues in the Conserved Sequence of the Catalytic Domain
Author:
Affiliation:
1. The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China
2. School of Biotechnology, Jiangnan University, Wuxi 214122, China
Funder
Ministry of Science and Technology of the People's Republic of China
Natural Science Foundation of Jiangsu Province
National Natural Science Foundation of China
Higher Education Discipline Innovation Project
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.2c01699
Reference40 articles.
1. Production, properties, and applications of fructosyltransferase: a current appraisal
2. Overproduction, purification, and property analysis of an extracellular recombinant fructosyltransferase
3. Immobilization of fructosyltransferase from Pichia pastoris in blend of alginate and gelatin
4. Recent Trends in Fructooligosaccharides Production
5. Heterologous expression and enzymatic characterization of fructosyltransferase from Aspergillus niger in Pichia pastoris
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