Enhanced thermostability of <i>Streptomyces mobaraensis</i> transglutaminase <i>via</i> computation-aided site-directed mutations and structural analysis-Reference-Cited by-同舟云学术

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Enhanced thermostability of Streptomyces mobaraensis transglutaminase via computation-aided site-directed mutations and structural analysis

Published:2024 Issue:2 Volume:48 Page:591-602
ISSN:1144-0546
Container-title:New Journal of Chemistry
language:en
Short-container-title:New J. Chem.

Author:

Li Yongzhen¹,Wu Banghao¹,Zhang Yumeng¹,Liu Lanxuan²,Bai Linquan¹^ORCID,Shi Ting¹^ORCID

Affiliation:

1. State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China

2. Digital Innovation of AI, WuXi Biologics, Shanghai 201400, China

Abstract

Streptomyces mobaraensis transglutaminase (smTG) has been widely used in the food processing industry for protein crosslinking.

Funder

National Natural Science Foundation of China

National Key Research and Development Program of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,General Chemistry,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2024/NJ/D3NJ04708C

Reference56 articles.

1. Plant Transglutaminases: New Insights in Biochemistry, Genetics, and Physiology

2. Approaching transglutaminase from Streptomyces bacteria over three decades

3. Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products

4. Versatility of Microbial Transglutaminase

5. Quality improvement of rice noodle restructured with rice protein isolate and transglutaminase

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