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槲皮素、芦丁与大豆分离蛋白非共价作用机制及其功能性和消化性研究 被引量:1

The Effect of Non-covalent Interaction of Soy Protein Isolate with Quercetin and Rutin on Functional Properties and in Vitro Digestion Characteristics
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摘要 本文分析了槲皮素-大豆分离蛋白与芦丁-大豆分离蛋白复合物功能性(溶解性、乳化性、凝胶性)和消化性的变化,并利用紫外可见光谱法、荧光光谱法研究互作机理,解析了其荧光淬灭类型、结合位点数以及热力学参数。结果发现,两种黄酮均可提高SPI的功能性质,当槲皮素与芦丁添加量分别为8%时,SPI凝胶硬度可分别提高23.23%及187.18%;随着槲皮素添加量的增加,SPI的EAI、ESI和溶解性先增加后趋于平缓,添加量为6%和4%时,乳化活性和溶解性分别达到最高,与SPI相比,分别提高20.84%和10.06%;随着芦丁添加量的增加,SPI的EAI、ESI和溶解性先增加后略有下降,在添加量为4%和6%时,乳化活性和溶解性分别达到最高,与SPI相比,分别提高26.17%和19.27%。此外,槲皮素、芦丁分别与SPI相互作用后还可提高蛋白的生物利用度,进一步研究两种黄酮多酚与SPI互作机制表明,两种互作复合物的荧光光谱均发生蓝移现象,槲皮素、芦丁与SPI自发结合,并主要通过氢键和范德华力方式作用,其中槲皮素、芦丁与SPI互作机制分别为动态淬灭及静态淬灭。 The changes in functionality(solubility,emulsification,gelation)and digestibility of quercetin-soy protein isolate and rutin-soy protein isolate complexes were analyzed in this paper.The interaction was studied by UV-Vis spectroscopy and fluorescence spectroscopy.The mechanism,the type of fluorescence quenching,the number of binding sites and thermodynamic parameters were analyzed.The results showed that quercetin and rutin could improve the functional properties of SPI.When the addition of quercetin and rutin were 8%,the hardness of SPI gel could be increased by 23.23%and 187.18%,respectively.The EAI,ESI and solubility of SPI increased first and then tended to level off.When the addition amount was 6%and 4%,the emulsifying activity and solubility reached the highest respectively,which were increased by 20.84%and 10.06%compared with SPI.With the increase of rutin addition,the EAI,ESI and solubility of SPI first increased and then decreased slightly.When the addition amount was 4%and 6%,the emulsifying activity and solubility reached the highest respectively,which was 26.17%and 19.27%than that of SPI.In addition,the interaction of quercetin and rutin with SPI could also improve the bioavailability of the protein.Further research on the interaction mechanism between the two flavonoid polyphenols and SPI showed that the fluorescence spectra of the two interacting complexes were blue-shifted,quercetin,rutin and SPI spontaneously combine,and mainly acted through hydrogen bonding and van der Waals forces.The interaction mechanism of quercetin,rutin and SPI was dynamic quenching and static quenching,respectively.
作者 赵钜阳 袁惠萍 孙昕萌 金聪 ZHAO Juyang;YUAN Huiping;SUN Xinmeng;JIN Cong(College of Tourism and Cuisine,Harbin University of Commerce,Harbin 150030,China)
出处 《食品工业科技》 CAS 北大核心 2022年第15期73-80,共8页 Science and Technology of Food Industry
基金 黑龙江省普通本科高等学校青年创新人才培养计划(UNPYSCT-2020213) 哈尔滨商业大学“青年创新人才”支持计划项目(2019CX23) 哈尔滨商业大学博士科研启动项目(2019DS60) 烹饪科学四川省高等学校重点实验室资助项目(PRKX201901)。
关键词 槲皮素 芦丁 溶解性 乳化性 凝胶性 消化特性 非共价作用 quercetin rutin solubility emulsification gelation digestibility non-covalent interaction
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