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Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed Kernel
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Weiyun WANG1, 2, Ningyao HAN1, 2, Yifang GAO1, 3, Ping YU1, 3, Zheling ZENG1, 2, 4, Xianghui YAN1, 2, 4, *
Science and Technology of Food Industry | 2026, 47(5) : 249 - 258
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Science and Technology of Food Industry | 2026, 47(5): 249-258
• Processing Technology •
Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed Kernel
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Weiyun WANG1, 2, Ningyao HAN1, 2, Yifang GAO1, 3, Ping YU1, 3, Zheling ZENG1, 2, 4, Xianghui YAN1, 2, 4, *
Affiliations
  • 1State of Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China
  • 2College of Food Science and Technology, Nanchang University, Nanchang 330031, China
  • 3School of Chemistry and Chemical Engineering, Nanchang University, Nanchang 330031, China
  • 4Jiangxi Provincial Key Laboratory of Agrofood Safety and Quality, Nanchang 330047, China
Published: 2026-03-01 doi: 10.13386/j.issn1002-0306.2025030027
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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; substrate concentration of 2% (w/v), 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 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.

Cinnamomum camphora seed kernel  /  enzymatic hydrolysis  /  bioactive peptide  /  degree of hydrolysis  /  α-glucosidase inhibition rate  /  antioxidant activity  /  amino acid composition
王炜芸, 韩泞遥, 高艺芳, 余平, 曾哲灵, 鄢祥辉. 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. 食品工业科技, 2026 , 47 (5) : 249 -258 . DOI: 10.13386/j.issn1002-0306.2025030027
Weiyun WANG, Ningyao HAN, Yifang GAO, Ping YU, Zheling ZENG, Xianghui YAN. Optimizing the Preparation Process and Antioxidant Activity of α-Glucosidase Inhibitory Peptide from Cinnamomum camphora Seed Kernel[J]. Science and Technology of Food Industry, 2026 , 47 (5) : 249 -258 . DOI: 10.13386/j.issn1002-0306.2025030027
Appendix
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Year 2026 volume 47 Issue 5
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doi: 10.13386/j.issn1002-0306.2025030027
  • Receive Date：2025-03-05
  • Online Date：2026-10-24
  • Published：2026-03-01
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  • Received：2025-03-05
Affiliations
    1State of Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China
    2College of Food Science and Technology, Nanchang University, Nanchang 330031, China
    3School of Chemistry and Chemical Engineering, Nanchang University, Nanchang 330031, China
    4Jiangxi Provincial Key Laboratory of Agrofood Safety and Quality, Nanchang 330047, China
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表12种不同金属材料的力学参数
科
Family		 属数
Number of
genus		 种数
Number of
species		 占总种数比例
Percentage of
total species (%)		 属
Genus		 种数
Number of
species		 占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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