食品科学 ›› 2022, Vol. 43 ›› Issue (11): 19-28.doi: 10.7506/spkx1002-6630-20210415-219

• 基础研究 • 上一篇    下一篇

烤牛肉中碳点与消化蛋白酶相互作用机制

柳康静,宋玉昆,王海涛,乔凤至,侯率,谭明乾   

  1. (大连工业大学食品学院,食品交叉科学研究院,国家海洋食品工程技术研究中心,海洋食品精深加工协同创新中心,辽宁 大连 116034)
  • 出版日期:2022-06-15 发布日期:2022-06-30
  • 基金资助:
    国家自然科学基金面上项目(31872915)

Interaction Mechanism between Carbon Dots and Digestive Proteases in Roast Beef

LIU Kangjing, SONG Yukun, WANG Haitao, QIAO Fengzhi, HOU Shuai, TAN Mingqian   

  1. (National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Academy of Food Interdisciplinary Science, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China)
  • Online:2022-06-15 Published:2022-06-30

摘要: 近年来,食品热加工过程中所产生食源性碳点(carbon dots,CDs)对人体健康的潜在影响已引起了人们的关注。本实验以牛肉为原料,在280 ℃下烤制30 min并分离纯化出CDs,通过体外模拟消化、荧光光谱、同步荧光光谱、傅里叶变换红外光谱、热力学分析等考察CDs在消化过程中与消化蛋白酶(胃蛋白酶和胰蛋白酶)的相互作用机制。体外模拟消化结果显示CDs与消化蛋白酶可以发生相互作用。荧光光谱分析结果表明CDs以静态猝灭的方式猝灭消化蛋白酶的固有荧光,同步荧光光谱分析结果表明酪氨酸参与了相互作用。热力学分析结果表明CDs与消化蛋白酶的结合方式为静电或疏水相互作用,并且结合后会直接影响胃蛋白酶和胰蛋白酶的二级结构,当CDs浓度为1.0×10-5 mol/L时,胃蛋白酶和胰蛋白酶的相对活力分别下降至(61.11±7.36)%和(51.28±3.62)%,本研究结果可为评估内源性纳米粒子的安全性提供参考。

关键词: 烤牛肉;碳点;消化蛋白酶;相互作用

Abstract: In recent years, the potential impact of food-derived carbon dots (CDs) produced during the thermal processing of foods on human health has attracted the attention of many people. In this study, CDs were extracted and purified from beef roasted at 280 ℃ for 30 min and evaluated for its interaction with digestive proteases (pepsin and trypsin) by in vitro simulated digestion, fluorescence spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared (FTIR) spectroscopy and thermodynamic analysis. The results of simulated digestion in vitro showed that the CDs could interact with digestive proteases. Fluorescence spectroscopic analysis showed that the CDs statistically quenched the inherent fluorescence of digestive proteases. The synchronous fluorescence results demonstrated that tyrosine was involved in the interaction. The thermodynamic results showed that the binding mode of the CDs and digestive proteases was electrostatic or hydrophobic interaction, and the combination affected the secondary structure of pepsin and trypsin. After interaction with the CDs at 1.0 × 10-5 mol/L, the activities of pepsin and trypsin decreased to (61.11 ± 7.36)% and (51.28 ± 3.62)% of their original value, respectively.

Key words: roast beef; carbon dots; digestive proteases; interaction

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