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Flavour binding mechanism between a typical meat flavour compound (nonanal) and porcine myofibrillar proteins with consideration of conformational changes
Author(s) -
Han Yurui,
Shen Hui,
Zhao Mouming,
Sun Weizheng
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13784
Subject(s) - nonanal , chemistry , quenching (fluorescence) , circular dichroism , conformational change , flavour , binding constant , fluorescence , crystallography , photochemistry , binding site , stereochemistry , biochemistry , organic chemistry , physics , food science , quantum mechanics
Summary Flavour binding or release behaviour from the meat matrix is very important for its sensory properties. The interaction between flavour substance (nonanal) and myofibrillar proteins ( MP s) was investigated using protein fluorescence quenching at different temperatures. The results suggested that nonanal caused the fluorescence quenching mechanism of MP s combining dynamic and static quenching mode, and dynamic quenching played a dominant role. Nonanal mainly combined with tryptophan residues rather than tyrosine residues. The results of synchronous fluorescence spectra and circular dichroism ( CD ) revealed that the interaction between nonanal and MP s induced no significant conformational changes in MP s. The binding constant ( K ) and number of binding sites ( n ) (1.45–2.03) increased with temperature. The negative value of ∆G (−383.16 kJ mol −1 to −397.30 kJ mol −1 ) showed that the interaction of nonanal and MP s was spontaneous. The positive ∆H (180.18 kJ mol −1 , 181.48 kJ mol −1 ) and ∆S (696.17 J mol −1 K −1 , 688.32 J mol −1 K −1 ) indicated that the binding of nonanal to MP s driven by hydrophobic force.