Effects of deamidation by protein glutaminase on the flavor binding properties of pea protein isolate

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dc.contributor.authorPanatthida Siripitakpong
dc.contributor.authorThanakorn Wongprasert
dc.contributor.authorThanyada Rungrotmongkol
dc.contributor.authorInthawoot Suppavorasatit
dc.date.accessioned2026-05-08T19:26:28Z
dc.date.issued2026-2-1
dc.description.abstract° values suggested that the interactions are entropy-driven and primarily hydrophobic in nature, which was confirmed using molecular docking studies, with stronger bonding to vanillin observed for PPI than for deamidated PPI. Sensory evaluation revealed that deamidation promoted flavor release. Thus, PG deamidation enhances flavor delivery performance, positioning deamidated PPI as promising protein-based component for improving flavor interactions in food applications.
dc.identifier.doi10.1016/j.fochx.2026.103712
dc.identifier.urihttps://dspace.kmitl.ac.th/handle/123456789/20604
dc.publisherFood Chemistry X
dc.subjectProteins in Food Systems
dc.subjectGABA and Rice Research
dc.subjectFermentation and Sensory Analysis
dc.titleEffects of deamidation by protein glutaminase on the flavor binding properties of pea protein isolate
dc.typeArticle

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