Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties
(1) Background: Microbial transglutaminases (MTGase) catalyze protein crosslink. This is useful in the food industry to improve gelation, water holding capacity, and emulsifying capacity during foodstuff manufacturing. The production of MTGase in wild-type strains renders low yield and high costs of...
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MDPI AG
2022-10-01
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| Series: | Gels |
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| Online Access: | https://www.mdpi.com/2310-2861/8/10/674 |
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| author | Tiange Ma Xingjiang Li Manuel Montalbán-López Xuefeng Wu Zhi Zheng Dongdong Mu |
| author_facet | Tiange Ma Xingjiang Li Manuel Montalbán-López Xuefeng Wu Zhi Zheng Dongdong Mu |
| author_sort | Tiange Ma |
| collection | DOAJ |
| description | (1) Background: Microbial transglutaminases (MTGase) catalyze protein crosslink. This is useful in the food industry to improve gelation, water holding capacity, and emulsifying capacity during foodstuff manufacturing. The production of MTGase in wild-type strains renders low yield and high costs of downstream purification, limiting its industrial applications. (2) Methods: In this work, MTGase from <i>Bacillus amyloliquefaciens</i> BH072 (BaMTGase) has been heterologously expressed in <i>Lactococcus lactis</i>, using the signal peptide Usp45 to direct the secretion of recombinant BaMTGase out of the cell for easier purification. (3) Results: In these conditions, MTGase was purified with a high yield (48.7 ± 0.2 mg/L) and high enzyme activity (28.6 ± 0.5 U/mg). Next, BaMTGase was tested for industrial applications. Recombinant BaMTGase and commercial MTGase were used for SPI solution crosslinking. BaMTGase formed a harder gel with higher water-holding capacity and a dense and smooth gel microstructure. (4) Conclusions: This work provides an attractive food-grade cell factory for the food industry and offers a suitable chassis for MTGase production. |
| first_indexed | 2024-03-09T20:11:38Z |
| format | Article |
| id | doaj.art-646b9b799bab400eaafea8d0492b4410 |
| institution | Directory Open Access Journal |
| issn | 2310-2861 |
| language | English |
| last_indexed | 2024-03-09T20:11:38Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Gels |
| spelling | doaj.art-646b9b799bab400eaafea8d0492b44102023-11-24T00:14:05ZengMDPI AGGels2310-28612022-10-0181067410.3390/gels8100674Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel PropertiesTiange Ma0Xingjiang Li1Manuel Montalbán-López2Xuefeng Wu3Zhi Zheng4Dongdong Mu5Anhui Fermented Food Engineering Research Center, School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, ChinaAnhui Fermented Food Engineering Research Center, School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, ChinaDepartment of Microbiology, Faculty of Sciences, University of Granada, 18071 Granada, SpainAnhui Fermented Food Engineering Research Center, School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, ChinaSchool of Food and Biological Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei University of Technology, Hefei 230601, ChinaAnhui Fermented Food Engineering Research Center, School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China(1) Background: Microbial transglutaminases (MTGase) catalyze protein crosslink. This is useful in the food industry to improve gelation, water holding capacity, and emulsifying capacity during foodstuff manufacturing. The production of MTGase in wild-type strains renders low yield and high costs of downstream purification, limiting its industrial applications. (2) Methods: In this work, MTGase from <i>Bacillus amyloliquefaciens</i> BH072 (BaMTGase) has been heterologously expressed in <i>Lactococcus lactis</i>, using the signal peptide Usp45 to direct the secretion of recombinant BaMTGase out of the cell for easier purification. (3) Results: In these conditions, MTGase was purified with a high yield (48.7 ± 0.2 mg/L) and high enzyme activity (28.6 ± 0.5 U/mg). Next, BaMTGase was tested for industrial applications. Recombinant BaMTGase and commercial MTGase were used for SPI solution crosslinking. BaMTGase formed a harder gel with higher water-holding capacity and a dense and smooth gel microstructure. (4) Conclusions: This work provides an attractive food-grade cell factory for the food industry and offers a suitable chassis for MTGase production.https://www.mdpi.com/2310-2861/8/10/674<i>Lactococcus lactis</i>microbial transglutaminase (MTGase)SPI gel |
| spellingShingle | Tiange Ma Xingjiang Li Manuel Montalbán-López Xuefeng Wu Zhi Zheng Dongdong Mu Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties Gels <i>Lactococcus lactis</i> microbial transglutaminase (MTGase) SPI gel |
| title | Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties |
| title_full | Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties |
| title_fullStr | Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties |
| title_full_unstemmed | Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties |
| title_short | Secretion of <i>Bacillus amyloliquefaciens</i> Transglutaminase from <i>Lactococcus lactis</i> and Its Enhancement of Food Gel Properties |
| title_sort | secretion of i bacillus amyloliquefaciens i transglutaminase from i lactococcus lactis i and its enhancement of food gel properties |
| topic | <i>Lactococcus lactis</i> microbial transglutaminase (MTGase) SPI gel |
| url | https://www.mdpi.com/2310-2861/8/10/674 |
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