Enzymatic Preparation and Stability of Hypoglycemic Peptides from Hairtail Waste
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LI Wenzhu,
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CHEN Hongbin,
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ZHOU Ruibing,
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ZOU Qian,
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LI Cheng,
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ZHOU Xiaomin,
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LIU Yu,
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YU Zhongjie,
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SUN Di,
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YAN Xiaojun,
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MA Qingbao,
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JIANG Wei
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Abstract
In this study, hairtail by-products were used as raw materials to optimize the enzymatic hydrolysis conditions for preparing α-glucosidase (α-GLU) inhibitory peptides using flavourzyme, through single-factor experiments and response surface methodology. The optimal hydrolysis conditions were determined to be an enzymatic hydrolysis temperature of 55 ℃, pH8.0, enzymatic hydrolysis time of 5.3 h, and enzyme addition of 9620 U/g. Under these conditions, the α-GLU inhibition rate of the inhibitory peptide from hairtail waste (IPHW) reached 64.8%±0.6%. Molecular weight analysis indicated that IPHW was mainly composed of oligopeptides with molecular weights below 1000 Da, accounting for 89.5%. In vitro stability tests showed that IPHW exhibited high stability under neutral or mildly alkaline pH, non-high-temperature, UV-shielded, and metal ion-free conditions (Na+, Mg2+, and Al3+). After simulated gastrointestinal digestion, IPHW retained more than 85% of its inhibitory activity, demonstrating good digestive stability. These results provide a novel approach for the high-value utilization of hairtail by-products and offer a theoretical basis for the development of natural, safe, and effective α-GLU inhibitory hypoglycemic peptides.
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