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Probing the molecular forces involved in binding of selected volatile flavour compounds to salt-extracted pea proteins
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文摘

Molecular forces were probed using various bond disturbing agents.

Aromatic, ketone and ester flavours bound pea proteins non-covalently.

Aldehyde and disulfide flavours covalently interacted with pea proteins.

Sulfhydryl–disulfide interchange reactions contributed to disulfide retention.

A combination of forces was required to explain binding mechanisms.

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