Effects of microwave pretreatment and transglutaminase crosslinking on the gelation properties of soybean protein isolate and wheat gluten mixtures

J Sci Food Agric. 2016 Aug;96(10):3559-66. doi: 10.1002/jsfa.7541. Epub 2016 Jan 4.

Abstract

Background: The integration of soybean protein isolate (SPI) with wheat gluten (WG) crosslinked via microbial transglutaminase (MTGase) may enhance the formation of ϵ-(γ-glutamyl)lysine covalent bonds, because SPI is rich in lysine and WG contains more glutamine. Microwave pretreatment may accelerate enzymatic reactions. In this study, we aimed to elucidate the effects of microwave pretreatment on the gelation properties of SPI and WG crosslinked with MTGase.

Results: Interestingly, the gel strength, water-holding capacity (WHC) and storage modulus (G') values of MTGase-induced SPI/WG gels were dramatically improved with increasing microwave power. Moreover, the MTGase crosslinking reaction promoted the formation of disulfide bonds, markedly reducing the free SH group and soluble protein content of gels. Fourier transform infrared spectroscopic analysis of SPI/WG gels showed that microwave pretreatment increased the proportion of α-helices and β-turns and decreased the proportion of β-sheets. Results from scanning electron microscopy indicated that the MTGase-induced SPI/WG gels had denser and more homogeneous microstructures after microwave pretreatment.

Conclusion: The effect of microwave pretreatment is useful in advancing gelation characters of MTGase-induced SPI/WG gels and provides the possibility for expanding the application of food protein. © 2015 Society of Chemical Industry.

Keywords: gel properties; microbial transglutaminase; microwave; soybean protein isolate; wheat gluten.

MeSH terms

  • Dipeptides / chemistry
  • Gels
  • Glutens / chemistry*
  • Microwaves
  • Soybean Proteins / chemistry*
  • Transglutaminases / chemistry*
  • Triticum / chemistry*
  • Water / chemistry

Substances

  • Dipeptides
  • Gels
  • Soybean Proteins
  • Water
  • epsilon-(gamma-glutamyl)-lysine
  • Glutens
  • Transglutaminases