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首页> 外文期刊>International Journal of Medicinal Mushrooms >Purification and Characterization of a Novel Serine Protease from the Fruiting Bodies of a Rare Edible Medicinal Mushroom, Lyophyllum shimeji (Agaricomycetes)
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Purification and Characterization of a Novel Serine Protease from the Fruiting Bodies of a Rare Edible Medicinal Mushroom, Lyophyllum shimeji (Agaricomycetes)

机译：从稀有可食用的蘑菇蘑菇（Lyophyllum shimeji（Agaricomycetes）的子实体中纯化和表征新型丝氨酸蛋白酶

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摘要

In this study, a novel protease with a molecular mass of 30 kDa was purified from Lyophyllum shimeji using a purification procedure that involved anion exchange chromatography on a Q-Sepharose column, cation chromatography on an SP-Sepharose column, and gel filtration on a Superdex 75 column. The protease was purified 57-fold, and its specific activity was 6.67 U/mg. Its inner amino acid sequence, determined by liquid chromatography-tandem mass spectrometry, contains AASIIAVLVLSDK, which has 93% identity with the sequence of Hypsizygus marmoreus serine protease. The optimal reaction temperature and pH for L. shimeji protease were 50 degrees C and 10.0, respectively. It is an alkaline protease and has higher activity when the pH lies between 6.8 and 10.0. The K-m and V-max at 50 degrees C and pH 9.0 were 1.32 mg/mL and 454.55 mu g/mL/min, respectively. The activity of L. shimeji protease was significantly suppressed by Cd2+ Hg2+Cu2+, and Fe3+ ions, as well as by phenylmethylsufonyl fluoride; therefore, it is a serine protease.
机译：在这项研究中，使用纯化程序从Qyotolum shimeji纯化了一种分子量为30 kDa的新型蛋白酶，该纯化程序包括在Q-Sepharose柱上进行阴离子交换色谱，在SP-Sepharose柱上进行阳离子色谱以及在Superdex上进行凝胶过滤75列。将该蛋白酶纯化57倍，其比活性为6.67U / mg。通过液相色谱-串联质谱法测定的其内部氨基酸序列包含AASIAVLVLSKD，其与马氏丝酵母丝氨酸蛋白酶的序列具有93％的同一性。 Shimeji蛋白酶的最佳反应温度和pH分别为50摄氏度和10.0。它是一种碱性蛋白酶，在pH介于6.8和10.0之间时具有较高的活性。在50摄氏度和pH 9.0下的K-m和V-max分别为1.32 mg / mL和454.55μg / mL / min。 Cd2 + Hg2 + Cu2 +和Fe3 +离子以及苯甲基磺酰氟显着抑制了姬菇乳酸杆菌的活性。因此，它是一种丝氨酸蛋白酶。

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