Characterization of an intracellular aspartic protease (PsAPA) from Penicillium sp. XT7 and its application in collagen extraction

文献类型： 外文期刊

第一作者： Guo, Yujie

作者： Guo, Yujie;Li, Xia;Jia, Wei;Huang, Feng;Liu, Yunhe;Zhang, Chunhui

作者机构：

关键词： Intracellular aspartic protease; Penicillium sp.; Characterization; Collagen extraction; Yield

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2021 年 345 卷

页码：

收录情况： SCI

摘要： An intracellular aspartic protease, PsAPA, was identified from Penicillium sp. XT7. This protease was belonged to penicillopepsin and was expressed in Pichia pastoris GS115. The recombinant PsAPA had a specific activity of 4289.7 +/- 261.7 U/mg. The pH and temperature maxima of the enzyme were 3.0 and 30 degrees C, respectively. The PsAPA was stable in the pH range from 3.0 to 6.0 and was completely inactivated after incubation at 50 degrees C for 15 min. Presence of Mn2+ and Cu2+ increased the proteolytic activity and beta-mercaptoethanol and SDS showed inhibitory effects, whereas 0.05 M pepstatin A strongly inhibited it. PsAPA could effectively hydrolyze animal proteins, including myoglobin, and hemoglobin but not collagens. PsAPA increased the yield of collagen extraction compared to the acid extraction method. The above properties show that the novel low-temperature acidic protease, PsAPA, is comparable to commercial proteases (porcine pepsin) and has great potential for collagen extraction.

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