1. Effect of alkyl distribution in pyrazine on pyrazine flavor release in bovine serum albumin solution
- Author
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Zhenyu Wang, Chao Wu, Xianbing Xu, Yun-Jiao Ma, Song Liang, Ming Du, Jian-Hai Wu, and Li Xiang
- Subjects
chemistry.chemical_classification ,Quenching (fluorescence) ,Pyrazine ,Absorption spectroscopy ,biology ,General Chemical Engineering ,Tryptophan ,02 engineering and technology ,General Chemistry ,010402 general chemistry ,021001 nanoscience & nanotechnology ,01 natural sciences ,Medicinal chemistry ,0104 chemical sciences ,chemistry.chemical_compound ,chemistry ,biology.protein ,Tyrosine ,Bovine serum albumin ,0210 nano-technology ,Alkyl ,Flavor - Abstract
The flavor release mechanism related to the interaction of aroma compounds with proteins is still unclear. In this study, the interaction of protein with pyrazine homologues, such as 2-methylpyrazine (MP), 2,5-dimethylpyrazine (DP), 2,3,5-trimethylpyrazine (TRP) and 2,3,5,6-tetramethylpyrazine (TEP), was investigated to elucidate the effect of alkyl distribution in a pyrazine ring on its flavor release in bovine serum albumin (BSA) solution (pH 7.4). The results of SPME-GC-MS indicated that methyl distribution in a pyrazine ring significantly affected its release from BSA solution. The pyrazines released from BSA solution with an increasing order of MP, DP, TRP and TEP. The inhibition mechanism of alkyl-pyrazine release was further elucidated by the interaction between alkyl-pyrazines and BSA using multiple spectroscopic methods. The non-covalent interaction between alkyl-pyrazines and BSA was confirmed as the main interaction force by the value of the bimolecular quenching constant (Kq > 2 × 1010 L mol−1 s−1). A decrease in the hydrophobicity of the microenvironment between the alkyl-pyrazine and BSA was detected by synchronous fluorescence spectra, which revealed that alkyl-pyrazines were mainly bound on the sites of tyrosine and tryptophan in BSA. The UV-vis absorption spectra and circular dichromatic (CD) spectrum revealed that alkyl-pyrazines could induce polarity and conformation change of BSA. The above results indicated that the structure of the flavor homologues can affect their release in food matrices.
- Published
- 2019