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中国精品科技期刊2020
薛天睿,吕彬斐,张铭冉,等. 卵黄高磷蛋白α-淀粉酶抑制肽的制备、鉴定及酶抑制动力学分析[J]. 食品工业科技,2025,46(1):1−12. doi: 10.13386/j.issn1002-0306.2024010363.
引用本文: 薛天睿,吕彬斐,张铭冉,等. 卵黄高磷蛋白α-淀粉酶抑制肽的制备、鉴定及酶抑制动力学分析[J]. 食品工业科技,2025,46(1):1−12. doi: 10.13386/j.issn1002-0306.2024010363.
XUE Tianrui, LÜ Binfei, ZHANG Mingran, et al. Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides[J]. Science and Technology of Food Industry, 2025, 46(1): 1−12. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024010363.
Citation: XUE Tianrui, LÜ Binfei, ZHANG Mingran, et al. Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides[J]. Science and Technology of Food Industry, 2025, 46(1): 1−12. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024010363.

卵黄高磷蛋白α-淀粉酶抑制肽的制备、鉴定及酶抑制动力学分析

Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides

  • 摘要: 为探索卵黄高磷蛋白肽(phosvitin phosphopeptide,PPP)对α-淀粉酶的抑制作用,使其能够调控血糖水平从而缓解Ⅱ型糖尿病,本研究以α-淀粉酶抑制率为指标酶解卵黄高磷蛋白制备PPP,利用酶抑制动力学实验分析PPP对α-淀粉酶的抑制类型,采用液质联用鉴定后用分子对接筛选出高活性的α-淀粉酶抑制肽,最后验证其活性。结果表明,最优酶解条件为先经胰蛋白酶(加酶量7000 U/g)再经胃蛋白酶(加酶量60000 U/g)分别酶解6 h,制得的PPP在浓度7.81×10−3 mg/mL时具有最高α-淀粉酶抑制率(70.69±1.71)%。PPP对α-淀粉酶的抑制类型为混合型抑制。鉴定筛选出了两种新型的高活性α-淀粉酶抑制肽FGTEPDAK和IWGR,经验证其IC50值分别为(0.80±0.14)×10−3 mg/mL和(1.80±0.31)×10−3 mg/mL,远低于阳性对照阿卡波糖(3.17±0.47)×10−3 mg/mL。本研究揭示PPP可作为新型降糖物质,应用于缓解Ⅱ型糖尿病的功能性食品开发中。

     

    Abstract: To explore the inhibiting effect of phosvitin phosphopeptide (PPP) on α-amylase, enabling it to regulate blood glucose levels and alleviate type 2 diabetes mellitus. This study employed enzymatic hydrolysis of phosvitin with the inhibition rate of α-amylase as an index, followed by enzyme inhibition kinetics experiments to analyze the inhibitory type of PPP on α-amylase. LC-MS identification was conducted, and molecular docking was performed to screen for highly active α-amylase inhibitory peptides, which were subsequently validated. The results showed that optimal enzymatic hydrolysis conditions involved initial hydrolysis with trypsin (7000 U/g), followed by pepsin (60000 U/g) for 6 hours each. The prepared PPP exhibited the highest α-amylase inhibition rate (70.69±1.71)% at a concentration of 7.81×10−3 mg/mL. PPP acted as a mixed-type inhibitor. Two novel highly active α-amylase inhibitory peptides FGTEPDAK and IWGR were identified and screened, exhibiting IC50 values of (0.80±0.14)×10−3 mg/mL and (1.80±0.31)×10−3 mg/mL, respectively; both significantly lower than the positive control acarbose's IC50 value (3.17±0.47)×10−3 mg/mL. This study highlights the potential use of PPP as a new hypoglycemic substance in developing functional foods for alleviating type 2 diabetes mellitus.

     

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