食品科学 ›› 2026, Vol. 47 ›› Issue (6): 58-68.doi: 10.7506/spkx1002-6630-20250924-193

• 基础研究 • 上一篇    

汽爆豌豆蛋白肽Cr(III)螯合物制备、结构表征及体外生物活性分析

张燕青,李倩,乔明武,沈玥,李宁,黄现青,雷凤梅,宋莲军   

  1. (河南农业大学食品科学技术学院,河南省食品加工与流通安全控制工程技术研究中心,郑州市大豆深加工重点实验室,河南 郑州 450002)
  • 发布日期:2026-04-14
  • 基金资助:
    河南省科技攻关项目(252102110133)

Preparation, Structural Characterization and in Vitro Biological Activities of Steam Explosion Modified Pea Protein-Derived Peptide-Chromium(III) Chelate

ZHANG Yanqing, LI Qian, QIAO Mingwu, SHEN Yue, LI Ning, HUANG Xianqing, LEI Fengmei, SONG Lianjun   

  1. (Henan Province Engineering Research Center for Food Safety Control of Processing and Circulation, Key Laboratory for Deep Processing of Soybean in Zhengzhou, College of Food Science and Technology, Henan Agricultural University, Zhengzhou 450002, China)
  • Published:2026-04-14

摘要: 为探究汽爆豌豆蛋白肽Cr(III)螯合物(steam-exploded pea protein peptides-chromium(III) chelate,SEPPs-Cr(III))的制备工艺及生物活性,以汽爆豌豆蛋白肽(steam-exploded pea protein peptides,SEPPs)作为原料与Cr(III)进行螯合,以Cr(III)螯合率为指标,通过单因素试验和响应面试验确定SEPPs-Cr(III)的最佳制备条件,通过紫外-可见光谱、荧光光谱、傅里叶变换红外光谱、圆二色光谱、Zeta电位和粒径、扫描电子显微镜对螯合前后样品进行结构表征,并对其体外抗氧化活性和降糖活性进行评价。结果表明,SEPPs-Cr(III)的最佳制备条件为肽溶液与Cr(III)溶液体积比1∶3.7、pH 4.6、温度37.5 ℃、时间70 min,在此条件下螯合率达到(31.67±0.75)%。与SEPPs相比,SEPPs-Cr(III)粒径增大,表面负电荷数量明显降低,β-折叠含量增加,无规卷曲含量减少,呈现出粗糙、折叠且致密的颗粒状聚集体外貌形态。此外,Cr(III)主要与SEPPs肽链中的氨基、羰基和羧基结合,形成具有稳定结构的螯合物。体外生物活性结果表明,SEPPs-Cr(III)对1,1-二苯基-2-三硝基苯肼自由基和羟自由基的半抑制浓度分别为5.14 mg/mL和4.6 mg/mL,显著低于SEPPs的11.6 mg/mL和8.79 mg/mL,对α-淀粉酶和α-葡萄糖苷酶半抑制浓度分别为0.39 mg/mL和0.59 mg/mL,显著低于SEPPs的3.14 mg/mL和9.18 mg/mL。此外,SEPPs-Cr(III)的还原能力显著优于SEPPs。本研究结果可为开发有机补铬剂提供一定的理论依据。

关键词: 豌豆蛋白;蒸汽爆破;肽Cr(III)螯合物;工艺优化;结构表征;生物活性

Abstract: This study prepared chromium(III)-chelating peptides derived from steam-exploded pea protein (SEPPs-Cr(III)) and evaluated its biological activities. The preparation conditions were optimized by one-factor-at-a-time (OFAT) method and response surface methodology (RSM) using the chelation rate of chromium(III) as the response variable. The structures of steam-exploded pea protein-derived peptides (SEPPs) and SEPPs-Cr(III) were characterized by ultraviolet-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy, Fourier transform infrared (FTIR) spectroscopy, circular dichroism (CD) spectroscopy, zeta potential, particle size, and scanning electron microscopy (SEM). Their antioxidant and hypoglycemic activities in vitro were evaluated. The results showed that the optimal preparation conditions were determined as: peptide/chromium(III) volume ratio of 1:3.7, pH 4.6, temperature of 37.5 ℃, and reaction time of 70 min. Under these conditions, the chelation rate of chromium(III) was (31.67 ± 0.75)%. Compared with SEPPs, SEPPs-Cr(III) exhibited an increased particle size, significantly reduced amounts of negative surface charge, increased β-sheet content, and decreased random coil content, showing a rough, folded, and compact granular aggregate morphology. Spectral analysis confirmed that chromium(III) primarily bound to amino, carbonyl, and carboxyl groups in the SEPP peptide chain, forming stable chelate structures. In vitro bioactivity studies indicated that the half maximal inhibitory concentrations (IC50) of SEPPs-Cr(III) against 1,1-diphenyl-2-picrylhydrazylradical (DPPH) and hydroxyl radicals were 5.14 and 4.6 mg/mL, respectively, which were significantly lower than those of SEPPs (11.6 and 8.79 mg/mL). The IC50 against α-amylase and α-glucosidase were also significantly lower than those of SEPPs (0.39 versus 3.14 mg/mL and 0.59 versus 9.18 mg/mL). Furthermore, SEPPs-Cr(III) exhibited a significantly stronger reducing capability than SEPPs. The findings provide a theoretical basis for developing organic chromium(III) supplements.

Key words: pea protein; steam explosion; peptide-Cr(III) chelate; process optimization; structural characterization; biological activities

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