Effect of transglutaminase on gelation and functional proteins of mung bean protein isolate.

Food Chem

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:

Published: October 2024

AI Article Synopsis

  • The study focused on enhancing the gelation properties of mung bean protein using microbial transglutaminase (mTGase), which notably increased gel hardness and storage modulus at a high enzyme concentration (2 IU/g) after 3 hours.
  • Scanning electron microscopy revealed a denser, more cross-linked structure formed at this enzyme level, and the treated samples showed a tripled water-holding capacity compared to the control.
  • Additionally, mTGase treatment resulted in improved emulsifying activity, indicated by a more uniform lipid droplet distribution, making it beneficial for developing plant-based seafood products.

Article 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 m/g from 3.79 ± 0.01 m/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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Source
http://dx.doi.org/10.1016/j.foodchem.2024.139590DOI Listing

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