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首页> 美国卫生研究院文献>Biomolecules >Extraction of Cathepsin D-Like Protease from Neon Flying Squid (Ommastrephes bartramii) Viscera and Application in Antioxidant Hydrolysate Production
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Extraction of Cathepsin D-Like Protease from Neon Flying Squid (Ommastrephes bartramii) Viscera and Application in Antioxidant Hydrolysate Production

机译：霓虹蝇鱿鱼内脏组织蛋白酶D样蛋白酶的提取及其在抗氧化剂水解物中的应用

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摘要

A protease from neon flying squid (Ommastrephes bartramii) viscera (SVCE3(f)) was partially purified by isoelectric solubilization/precipitation combined with ultra-membrane filtration (ISP-UMF). Two protein bands of 45 and 27 KDa were determined by SDS-PAGE assay. The protease characteristic of the protein band of 45 KDa was confirmed using casein zymography analysis. The result of UPLC-ESI-MS/MS suggested that the band of 45 KDa could be a cathepsin D-like protease. This cathepsin D-like protease showed an optimum pH of 3.0 and optimum temperature of 60 °C when casein was used as s substrate. Furthermore, its protease activity was stable at 30–50 °C and under a pH range of 1.0–5.0, maintaining about 60% of its initial activity. SVCE3(f) can digest half-fin anchovy (Setipinna taty) to generate antioxidant hydrolysates (HAHp-SEs). The degree of hydrolysis (DH) of HAHp-SEs increased along with the hydrolysis time and reached stability after 60 min of digestion. HAHp-SEs(30) with relatively lower DH exhibited the highest DPPH radical scavenging activity as compared with other HAHp-SEs. However, a stronger hydroxyl radical scavenging activity and greater reducing power were observed for HAHp-SEs that underwent higher DH. Accordingly, the partially purified cathepsin D-like protease of neon flying squid viscera using ISP-UMF could have potential application in antioxidant hydrolysates production.
机译：通过等电增溶/沉淀结合超膜过滤（ISP-UMF），部分纯化了来自飞乌贼（Ommastrephes bartramii）内脏的蛋白酶（SVCE3（f））。通过SDS-PAGE测定法确定了45和27KDa的两个蛋白带。用酪蛋白酶谱分析证实了45KDa蛋白带的蛋白酶特征。 UPLC-ESI-MS / MS的结果表明45 KDa的条带可能是组织蛋白酶D样蛋白酶。当酪蛋白用作底物时，该组织蛋白酶D样蛋白酶显示最佳pH为3.0，最佳温度为60℃。此外，其蛋白酶活性在30–50°C和1.0–5.0的pH范围内稳定，保持其初始活性的约60％。 SVCE3（f）可以消化半翅an鱼（Setipinna taty）以产生抗氧化剂水解物（HAHp-SEs）。 HAHp-SEs的水解度（DH）随水解时间的增加而增加，并在60分钟的消化后达到稳定。与其他HAHp-SEs相比，DH相对较低的HAHp-SEs（30）表现出最高的DPPH自由基清除活性。然而，观察到DH较高的HAHp-SEs具有更强的羟基自由基清除活性和更大的还原能力。因此，使用ISP-UMF部分纯化的飞鱿鱼内脏的组织蛋白酶D样蛋白酶可能在抗氧化剂水解产物的生产中具有潜在的应用。

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