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中国精品科技期刊2020
王炜芸,韩泞遥,高艺芳,等. 樟树籽仁源α-葡萄糖苷酶抑制肽的制备工艺优化及其抗氧化活性J. 食品工业科技,2026,47(5):1−10. doi: 10.13386/j.issn1002-0306.2025030027.
引用本文: 王炜芸,韩泞遥,高艺芳,等. 樟树籽仁源α-葡萄糖苷酶抑制肽的制备工艺优化及其抗氧化活性J. 食品工业科技,2026,47(5):1−10. doi: 10.13386/j.issn1002-0306.2025030027.
WANG Weiyun, HAN Ningyao, GAO Yifang, et al. Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed KernelJ. Science and Technology of Food Industry, 2026, 47(5): 1−10. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025030027.
Citation: WANG Weiyun, HAN Ningyao, GAO Yifang, et al. Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed KernelJ. Science and Technology of Food Industry, 2026, 47(5): 1−10. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025030027.

樟树籽仁源α-葡萄糖苷酶抑制肽的制备工艺优化及其抗氧化活性

Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed Kernel

  • 摘要: 为高值化开发利用我国资源丰富的樟树籽、筛选樟树籽仁源α-葡萄糖苷酶抑制肽,本研究以樟树籽仁蛋白为原料,采用水解度(DH)和α-葡萄糖苷酶抑制率作为评价指标,通过单因素和正交试验优化制备得到樟树籽仁源α-葡萄糖苷酶抑制肽,并测定分析其氨基酸组成和体外抗氧化活性。结果表明,樟树籽仁源α-葡萄糖苷酶抑制肽的最优酶解工艺为:以木瓜蛋白酶为水解酶,底物浓度为2%(w/v)、酶解温度为55 ℃、酶解pH为6.0、酶解时间为2.0 h、酶添加量为16000 U/g,该条件下樟树籽仁蛋白酶解物的DH值为26.81%。制得的樟树籽仁源α-葡萄糖苷酶抑制肽对α-葡萄糖苷酶、DPPH自由基和ABTS+自由基的半数抑制率(IC50值)分别为11.52、5.42和0.64 mg/mL。本研究为樟树籽仁源α-葡萄糖苷酶抑制肽的挖掘提供了理论依据。

     

    Abstract: To achieve high-value development and use of the abundant Cinnamomum camphora seed resources in China and screen the α-glucosidase inhibitor peptides derived from Cinnamomum camphora seed kernel (CCSK), the aim of this study was to produce α-glucosidase inhibitory peptides from CCSK by optimizing CCSK protein enzymatic hydrolysis conditions through single-factor experiments and orthogonal tests. Degree of hydrolysis (DH) and α-glucosidase inhibitory activity were used as evaluation indexes. Subsequently, the amino acid composition and in vitro antioxidant activity of the obtained α-glucosidase inhibitory peptides were analyzed. The results revealed that the following were the optimal conditions of CCSK protein enzymatic hydrolysis: papain as the hydrolase; hydrolysis temperature of 55 ℃, pH of 6.0, hydrolysis duration of 2.0 h, and an enzyme addition of 16000 U/g. At these conditions, the DH value of the obtained CCSK α-glucosidase inhibitory peptides was 26.81%, while their median inhibition rates (IC50 values) on α-glucosidase, DPPH free radicals, and ABTS+ free radicals were 11.52, 5.42, and 0.64 mg/mL, respectively. This study provides a theoretical basis for production of α-glucosidase inhibitory peptides from CCSK.

     

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