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Effect of transglutaminase on gelation and functional proteins of mung bean protein isolate.
Vijayan, Poornima; Song, Zhixuan; Toy, Joanne Yi Hui; Yu, Liangli Lucy; Huang, Dejian.
Affiliation
  • Vijayan P; Department of Food Science & Technology, National University of Singapore, 2 Science Drive 2, Singapore 117542, Singapore.
  • Song Z; Department of Food Science & Technology, National University of Singapore, 2 Science Drive 2, Singapore 117542, Singapore.
  • Toy JYH; Department of Food Science & Technology, National University of Singapore, 2 Science Drive 2, Singapore 117542, Singapore.
  • Yu LL; Department of Food Science and Nutrition, University of Maryland, College Park, MD 20742 USA.
  • Huang D; Department of Food Science & Technology, National University of Singapore, 2 Science Drive 2, Singapore 117542, Singapore; National University of Singapore (Suzhou) Research Institute, 377 Lin Quan Street, Suzhou Industrial Park, Suzhou, Jiangsu 215123, China. Electronic address: dejian@nus.edu.
Food Chem ; 454: 139590, 2024 Oct 01.
Article in En | MEDLINE | ID: mdl-38823202
ABSTRACT
This study aimed to improve mung bean protein's gelation qualities via microbial transglutaminase (mTGase) cross-linking. The mTGase treatment significantly improved gel hardness and storage modulus (G') at higher enzyme levels (2 IU/g), peaking hardness at 3 h. The scanning electron microscopy imaging demonstrated more cross-linked structures at 2 IU/g, evolving into a dense network by 3 h. The water-holding capacity for mTGase-treated samples (2 IU/g, 3 h, 55 °C) tripled to 3.77 ± 0.06 g/g versus control (1.24 ± 0.02 g/g), alongside a 15 % decrease in zeta potential (-30.84 ± 0.901 mV versus control's -26.63 ± 0.497 mV) and an increase in emulsifying activity index to 4.519 ± 0.004 m2/g from 3.79 ± 0.01 m2/g (control). The confocal images showed a more uniform lipid droplet distribution in mTGase-treated samples, suggesting enhanced emulsifying activity. Thus, mTGase treatment significantly improved gel strength and emulsifying properties, making it ideal for plant-based seafood products.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins / Transglutaminases / Vigna / Gels Language: En Journal: Food Chem Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins / Transglutaminases / Vigna / Gels Language: En Journal: Food Chem Year: 2024 Document type: Article Affiliation country: