从青霉 XT7 中鉴定一种细胞内天冬氨酸蛋白酶（PsAPA）及其在胶原蛋白提取中的应用。
Characterization of an intracellular aspartic protease (PsAPA) from Penicillium sp. XT7 and its application in collagen extraction.
机构信息
Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
出版信息
Food Chem. 2021 May 30;345:128834. doi: 10.1016/j.foodchem.2020.128834. Epub 2020 Dec 8.
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 °C, respectively. The PsAPA was stable in the pH range from 3.0 to 6.0 and was completely inactivated after incubation at 50 °C for 15 min. Presence of Mn and Cu increased the proteolytic activity and β-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.
从青霉属 XT7 中鉴定出一种细胞内天冬氨酸蛋白酶 PsAPA。该蛋白酶属于青霉素酶，在毕赤酵母 GS115 中表达。重组 PsAPA 的比活为 4289.7±261.7 U/mg。该酶的最适 pH 和温度分别为 3.0 和 30°C。该酶在 pH 3.0 至 6.0 范围内稳定，在 50°C 孵育 15 分钟后完全失活。Mn 和 Cu 的存在增加了酶的蛋白水解活性，β-巯基乙醇和 SDS 显示出抑制作用，而 0.05 M 胃蛋白酶抑制剂 A 则强烈抑制其活性。PsAPA 可以有效水解动物蛋白，包括肌红蛋白和血红蛋白，但不能水解胶原蛋白。与酸提取方法相比，PsAPA 提高了胶原蛋白提取的产量。上述特性表明，新型低温酸性蛋白酶 PsAPA 可与商业蛋白酶（猪胃蛋白酶）相媲美，在胶原蛋白提取方面具有巨大潜力。
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