alcalase酶水解提高水稻分离蛋白的功能特性及其生物活性评价

JSFA reports Pub Date : 2023-07-13 DOI:10.1002/jsf2.140
Kavitha Susan Issac, Shubha Banerjee, Sahayog N. Jamdar
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引用次数: 0

摘要

利用过剩的稻谷提高生产力,开发稻谷增值产品变得越来越重要。因此,本研究的目的是通过酶解提高4个水稻品种(RRF-127、RRF-105、Swarna和Protezin)水稻蛋白的功能特性,并评价其水解产物的抗氧化、ACE和DPP-IV抑制活性等生物活性。结果在4 ~ 10的pH范围内,alcalase水解使蛋白溶解度提高到80%。随着pH值的增加,大米蛋白水解物(RPHs)的发泡能力和稳定性得到改善,在pH值为5 ~ 9的范围内,大米蛋白水解物的乳化活性指数(EAI)显著提高。水解产物具有抗氧化活性,即清除ABTS•+自由基、还原能力和金属离子螯合能力。结果表明,RRF-105具有较强的抗氧化能力。RPH能减轻红细胞氧化损伤,其保护作用呈浓度依赖性。水解产物对ACE和DPP-IV酶有较强的抑制作用。Protezin表现出最高的ACE抑制(63%),而Swarna表现出最有效的DPP-IV抑制(66%)。结论alcalase水解提高了水稻蛋白的功能和生物活性,表明RPH可以作为生物活性肽的来源或作为具有潜在功能的功能成分。
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Improving functional properties of rice protein isolates by hydrolysis using alcalase enzyme and assessing bioactivities of hydrolysates

Background

Developing value-added products from rice grains is becoming increasingly significant to enhance productivity from excess rice grains. Therefore, the objective of this study was to improve the functional properties of rice protein from four rice varieties, namely, RRF-127, RRF-105, Swarna, and Protezin by enzymatic hydrolysis, and also to evaluate bioactivities like antioxidant, ACE, and DPP-IV inhibitory activities of the hydrolysates.

Results

The alcalase hydrolysis increased protein solubility to >80% in the pH range of 4–10. The foaming capacity and stability of rice protein hydrolysates (RPHs) improved with the increase in pH. The hydrolysis significantly improved the emulsification activity index (EAI) in the pH range of 5–9. The hydrolysates showed antioxidant activity, namely, ABTS+radical scavenging, reducing power, and metal ion chelation. RRF-105 was found to possess the most potent antioxidant capacity among the hydrolysates. RPH could alleviate oxidative damage in erythrocytes, and their protective effects were concentration-dependent. The hydrolysates had stronger inhibition of ACE and DPP-IV enzymes. Protezin exhibited the highest ACE inhibition (63%), while Swarna demonstrated the most effective DPP-IV inhibition (66%).

Conclusion

Hydrolysis with alcalase improved the functional and bioactive properties of rice proteins, indicating that RPH could serve as a source of bioactive peptides or as a functional ingredient with potential properties.

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