TY - JOUR
T1 - Non-covalent binding of chlorogenic acid to myofibrillar protein improved its bio-functionality properties and metabolic fate
AU - Zhou, Zhiwei
AU - Wang, Dan
AU - Luo, Dongmei
AU - Zhou, Zhiqiang
AU - Liu, Wei
AU - Zeng, Weicai
AU - Dinnyés, András
AU - Xiong, Youling L.
AU - Sun, Qun
N1 - Publisher Copyright:
© 2023 Elsevier Ltd
PY - 2024/5/15
Y1 - 2024/5/15
N2 - As natural antioxidants added to meat products, polyphenols can interact with proteins, and the acid-base environment influenced the extent of non-covalent and covalent interactions between them. This study compared the bio-functional characteristics and metabolic outcomes of the myofibrillar protein-chlorogenic acid (MP-CGA) complexes binding in different environments (pH 6.0 and 8.5). The results showed that CGA bound with MP significantly enhanced its antioxidant activity and inhibitory effect on metabolism enzymes. CGA bound deeply into the MP structure hydrophobic cavity at pH 6.0, which reduced its degradation by digestive enzymes, thus increasing its bio-accessibility from 59.5% to 71.6%. The digestion products of the two complexes exhibited significant differences, with the non-covalent MP-CGA complexes formed at pH 6.0 showing significantly higher concentrations of rhetsinine and piplartine, two well-known compounds to modulate diabetes. This study demonstrated that non-covalent binding between protein and polyphenol in the acidic environment held greater promising prospects for improving health.
AB - As natural antioxidants added to meat products, polyphenols can interact with proteins, and the acid-base environment influenced the extent of non-covalent and covalent interactions between them. This study compared the bio-functional characteristics and metabolic outcomes of the myofibrillar protein-chlorogenic acid (MP-CGA) complexes binding in different environments (pH 6.0 and 8.5). The results showed that CGA bound with MP significantly enhanced its antioxidant activity and inhibitory effect on metabolism enzymes. CGA bound deeply into the MP structure hydrophobic cavity at pH 6.0, which reduced its degradation by digestive enzymes, thus increasing its bio-accessibility from 59.5% to 71.6%. The digestion products of the two complexes exhibited significant differences, with the non-covalent MP-CGA complexes formed at pH 6.0 showing significantly higher concentrations of rhetsinine and piplartine, two well-known compounds to modulate diabetes. This study demonstrated that non-covalent binding between protein and polyphenol in the acidic environment held greater promising prospects for improving health.
KW - Bio-functional properties
KW - Chlorogenic acid
KW - Metabolic fate
KW - Non-covalent binding
KW - Polyphenol bio-accessibility
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U2 - 10.1016/j.foodchem.2023.138208
DO - 10.1016/j.foodchem.2023.138208
M3 - Article
C2 - 38159322
AN - SCOPUS:85181104373
SN - 0308-8146
VL - 440
JO - Food Chemistry
JF - Food Chemistry
M1 - 138208
ER -