Effect of incubation temperature on the binding capacity of flavor compounds to myosin

被引：48

作者：

He, Yujia ^{[1
]}

Zhou, Changyu ^{[1
]}

Li, Chunbao ^{[1
]}

Zhou, Guanghong ^{[1
]}

机构：

[1] Nanjing Agr Univ, Jiangsu Synerget Innovat Ctr Meat Proc & Qual Con, Key Lab Meat Proc & Qual Control, MOE,Key Lab Meat Proc,MOA, Nanjing 210095, Peoples R China

来源：

FOOD CHEMISTRY | 2021年 / 346卷

关键词：

Myosin; Aldehydes; Temperature; Binding capacity; Flavor; ISOTHERMAL TITRATION CALORIMETRY; VOLATILE COMPOUNDS; AROMA COMPOUNDS; HEAT-TREATMENT; SERUM-ALBUMIN; SOY PROTEIN; G-ACTIN; MECHANISM; CANOLA; HAM;

D O I：

10.1016/j.foodchem.2020.128976

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This study was aimed to investigate the effect of incubation temperature on the binding of hexanal, octanal and 3-methylbutyraldehyde to myosin. Fluorescence quenching, Fourier transform infrared spectroscopy, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC) and gas chromatography-mass spectrometry (GC-MS) were employed. An increase in aldehyde concentration led to a reduction in fluorescence intensity in myosin. SPR revealed that the interactions were involved in a rapid combination and dissociation, and the dissociation constants significantly decreased from 25 to 37 degrees C. ITC showed that the values of entropy, enthalpy and Gibbs free energy were negative. The interactions were driven by hydrogen bonds and van der Waals forces. GC-MS further demonstrated that the highest binding capacity occurred at 37 degrees C between myosin and aldehydes. The findings provide a new insight into the mechanism on controlling or maintaining meat flavor.

引用

页数：8

共 38 条

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