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Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins
Until now, Streptoverticillium mobaraense transglutaminase (TG) is the only commercialized TG, but limited information is known about its selection tendency on crosslinking sites at the protein level, restricting its application in the food industry. Here, four recombinant Bacillus TGs were stable i...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9689123/ https://www.ncbi.nlm.nih.gov/pubmed/36429314 http://dx.doi.org/10.3390/foods11223722 |
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author | Wang, Hongbin Zhang, Yuanfu Yuan, Zhaoting Zou, Xiaotong Ji, Yuan Hou, Jiayi Zhang, Jinfang Lu, Fuping Liu, Yihan |
author_facet | Wang, Hongbin Zhang, Yuanfu Yuan, Zhaoting Zou, Xiaotong Ji, Yuan Hou, Jiayi Zhang, Jinfang Lu, Fuping Liu, Yihan |
author_sort | Wang, Hongbin |
collection | PubMed |
description | Until now, Streptoverticillium mobaraense transglutaminase (TG) is the only commercialized TG, but limited information is known about its selection tendency on crosslinking sites at the protein level, restricting its application in the food industry. Here, four recombinant Bacillus TGs were stable in a broad range of pH (5.0–9.0) and temperatures (<50 °C), exhibiting their maximum activity at 50–60 °C and pH 6.0–7.0. Among them, TG of B. cereus (BCETG) demonstrated the maximal specific activity of 177 U/mg. A structural analysis indicated that the Ala147-Ala156 region in the substrate tunnel of BCETG played a vital role in catalytic activity. Furthermore, bovine serum albumin, as well as nearly all protein ingredients in soy protein isolate and whey protein, could be cross-linked by BCETG, and the internal crosslinking paths of three protein substrates were elucidated. This study demonstrated Bacillus TGs are a candidate for protein crosslinking and provided their crosslinking mechanism at the protein level for applications in food processing. |
format | Online Article Text |
id | pubmed-9689123 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96891232022-11-25 Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins Wang, Hongbin Zhang, Yuanfu Yuan, Zhaoting Zou, Xiaotong Ji, Yuan Hou, Jiayi Zhang, Jinfang Lu, Fuping Liu, Yihan Foods Article Until now, Streptoverticillium mobaraense transglutaminase (TG) is the only commercialized TG, but limited information is known about its selection tendency on crosslinking sites at the protein level, restricting its application in the food industry. Here, four recombinant Bacillus TGs were stable in a broad range of pH (5.0–9.0) and temperatures (<50 °C), exhibiting their maximum activity at 50–60 °C and pH 6.0–7.0. Among them, TG of B. cereus (BCETG) demonstrated the maximal specific activity of 177 U/mg. A structural analysis indicated that the Ala147-Ala156 region in the substrate tunnel of BCETG played a vital role in catalytic activity. Furthermore, bovine serum albumin, as well as nearly all protein ingredients in soy protein isolate and whey protein, could be cross-linked by BCETG, and the internal crosslinking paths of three protein substrates were elucidated. This study demonstrated Bacillus TGs are a candidate for protein crosslinking and provided their crosslinking mechanism at the protein level for applications in food processing. MDPI 2022-11-19 /pmc/articles/PMC9689123/ /pubmed/36429314 http://dx.doi.org/10.3390/foods11223722 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Hongbin Zhang, Yuanfu Yuan, Zhaoting Zou, Xiaotong Ji, Yuan Hou, Jiayi Zhang, Jinfang Lu, Fuping Liu, Yihan Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title | Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title_full | Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title_fullStr | Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title_full_unstemmed | Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title_short | Crosslinking Mechanism on a Novel Bacillus cereus Transglutaminase-Mediated Conjugation of Food Proteins |
title_sort | crosslinking mechanism on a novel bacillus cereus transglutaminase-mediated conjugation of food proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9689123/ https://www.ncbi.nlm.nih.gov/pubmed/36429314 http://dx.doi.org/10.3390/foods11223722 |
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