Enhancing the functional characteristics of soy protein isolate via cross‐linking catalyzed by Bacillus subtilis transglutaminase
BACKGROUND Although Streptomyces mobaraense transglutaminase (MTG) has been extensively applied to enhance the functional characteristics of soy protein isolate (SPI) through cross‐linking, various transglutaminases (TGs) in nature may provide more choice in the food industry. Previous research repo...
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Veröffentlicht in: | Journal of the science of food and agriculture 2021-08, Vol.101 (10), p.4154-4160 |
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Hauptverfasser: | , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | BACKGROUND
Although Streptomyces mobaraense transglutaminase (MTG) has been extensively applied to enhance the functional characteristics of soy protein isolate (SPI) through cross‐linking, various transglutaminases (TGs) in nature may provide more choice in the food industry. Previous research reported that TG derived from Bacillus subtilis (BTG) exhibited better pH stability and thermostability than MTG.
RESULTS
An attempt was made to study the influence of BTG induced cross‐linking on the properties of SPI. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) results indicated that almost all protein constituents (α', α, β, AS, and BS) in SPI could be cross‐linked with BTG treatment. The BTG treatment also resulted in a significant increase (*P |
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ISSN: | 0022-5142 1097-0010 |
DOI: | 10.1002/jsfa.11052 |