茶叶籽粕蛋白酶解物的抗氧化及抑制α-葡萄糖苷酶活性研究

陈巧玲; 卢学慧; 王弛; 赵峰

doi:10.20045/j.cnki.issn.2096-0220.2024.02.008

茶叶籽粕蛋白酶解物的抗氧化及抑制α-葡萄糖苷酶活性研究

Antioxidative and Anti-α-glucosidase Activities of Enzymatically Hydrolyzed Tea Seed Protein

摘要

摘要:
目的提取茶叶籽粕蛋白，并比较其经不同蛋白酶酶解后的抗氧化活性和α-葡萄糖苷酶抑制率，进而评估将其作为新型生物活性肽生产原料的可行性。
方法首先通过碱提酸沉法获得茶叶籽粕蛋白粗提物，再分别以碱性蛋白酶、中性蛋白酶和木瓜蛋白酶进行酶解；比较各酶解物的DPPH自由基清除率、ABTS自由基清除率、总还原力和α-葡萄糖苷酶抑制率的差异。
结果采用碱提酸沉法（0.1 mol·L⁻¹ NaOH提取、1 mol·L⁻¹ HCl调整pH至3.5）制备的茶叶籽粕蛋白粗提物，其得率为7.7%，蛋白纯度27.6%。酶解物活性评价结果显示，碱性蛋白酶酶解物对DPPH自由基清除率最高，其IC₅₀（半数抑制浓度）为80.17 μg·mL⁻¹；对ABTS自由基清除率最高，其IC₅₀为123.79 μg·mL⁻¹；总还原力最强，为0.458；浓度为1 mg·mL⁻¹时对α-葡萄糖苷酶抑制率较强，为93.12%。
结论采用碱性蛋白酶酶解茶叶籽粕蛋白粗提物，其酶解物具有开发成抗氧化和抑制α-葡萄糖苷酶生物活性肽的潜力。

Abstract:
Objective Antioxidative and anti-α-glucosidase activities of enzymatically hydrolyzed protein extracted from tea seed meal were determined for the development of a functional peptide product.
Method Camellia sinensis seed meal was alkaline-extracted using 0.1 mol·L⁻¹ NaOH and followed by acid precipitation with 1 mol·L⁻¹ HCl at pH 3.5 to obtain crude protein which was subsequently enzymatically hydrolyzed. The hydrolysates produced by applying alcalase, a neutral protease, or papain were tested for DPPH and ABTS free radical scavenging capacities as well as reducing power and α-glucosidase inhibition.
Result The tea seed protein extraction process yielded 7.7% solids that contained 27.6% protein. Among the 3 proteases, alacase delivered a hydrolysate with the highest IC₅₀ of 80.17 μg·mL⁻¹ in scavenging DPPH free radicals and an IC₅₀ of 123.79 μg·mL⁻¹ in scavenging ABTS free radicals. The hydrolysate also showed the greatest total reducing power of 0.458 and α-glucosidase inhibition rate of 93.12% at an applied concentration of 1 mg·mL⁻¹.
Conclusion The alacase-hydrolyzed tea seed protein exhibited significant in vitro free radical scavenging and anti-α-glucosidase activities of a bioactive peptide.

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