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来自URM 4133的一种新型丝氨酸蛋白酶的生化和热力学特性

Biochemical and thermodynamic characteristics of a new serine protease from URM 4133.

作者信息

Gomes José Erick Galindo, Rosa Isabel Zaparoli, Nascimento Talita Camila Evaristo da Silva, Souza-Motta Cristina Maria de, Gomes Eleni, Boscolo Mauricio, Moreira Keila Aparecida, Pintado Maria Manuela Estevez, da Silva Roberto

机构信息

São Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (IBILCE), Cristovão Colombo, 2265, Jardim Nazareth, 15054-000, Campus São José do Rio Preto, São Paulo, Brazil.

Laboratory of Microbiology, Enzymatic Technology and Bioproducts, Academic Unit of Garanhuns, Federal Rural University of Pernambuco (UFRPE), Bom Pastor Avenue, Garanhuns, Pernambuco, Brazil.

出版信息

Biotechnol Rep (Amst). 2020 Nov 4;28:e00552. doi: 10.1016/j.btre.2020.e00552. eCollection 2020 Dec.

DOI:10.1016/j.btre.2020.e00552
PMID:33294402
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7683317/
Abstract

A protease from the fungus URM 4133, capable of producing bioactive peptides from goat casein, was purified. SDS-PAGE and zymography showed a molecular mass of 30 kDa. The enzyme was active and stable in a wide pH range (6.0-10.5) and (5.0-10.5), respectively. Optimum temperature was at 45-50 °C and stability was above 80 % (40 °C/2 h). Activity was not influenced by ions or organic substances (Triton, Tween, SDS and DMSO), but was completely inhibited by PMSF, suggesting that it belongs to the serine protease family. The Km and Vmax were 2.35 mg azocasein.mL-1 and 333.33 U.mg protein-1, respectively. Thermodynamic parameters of irreversible denaturation (40-60 °C) were enthalpy 123.63 - 123.46 kJ.mol-1, entropy 120.24-122.28 kJ.mol-1 and Gibbs free energy 85.97 - 82.45 kJ.mol-1. Any peptide sequences compatible with this protease were found after analysis by MALDI-TOF, which suggests that it is a new serine protease.

摘要

一种来自真菌URM 4133的蛋白酶被纯化出来，它能够从山羊酪蛋白中产生生物活性肽。SDS-PAGE和酶谱分析显示其分子量为30 kDa。该酶分别在较宽的pH范围（6.0 - 10.5）和温度范围（5.0 - 10.5）内具有活性且稳定。最适温度为45 - 50 °C，在40 °C下2小时的稳定性高于80%。其活性不受离子或有机物质（Triton、吐温、SDS和DMSO）的影响，但被PMSF完全抑制，这表明它属于丝氨酸蛋白酶家族。Km和Vmax分别为2.35 mg偶氮酪蛋白·mL-1和333.33 U·mg蛋白-1。不可逆变性（40 - 60 °C）的热力学参数为焓123.63 - 123.46 kJ·mol-1、熵120.24 - 122.28 kJ·mol-1和吉布斯自由能85.97 - 82.45 kJ·mol-1。经基质辅助激光解吸电离飞行时间质谱（MALDI-TOF）分析后未发现与该蛋白酶兼容的任何肽序列，这表明它是一种新型丝氨酸蛋白酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/c36f17ddd2f2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/16839f8d2749/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/484a1e03ed5f/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/33f52a4434ee/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/08bed86c3ead/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/1511304f36e2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/97f6df4cbd70/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/c36f17ddd2f2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/16839f8d2749/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/484a1e03ed5f/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/33f52a4434ee/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/08bed86c3ead/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/1511304f36e2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/97f6df4cbd70/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/086a/7683317/c36f17ddd2f2/gr6.jpg

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