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一株降解角蛋白的黑曲霉产蛋白水解酶的研究

Production of Proteolytic Enzymes by a Keratin-Degrading Aspergillus niger.

作者信息

Lopes Fernanda Cortez, Silva Lucas André Dedavid E, Tichota Deise Michele, Daroit Daniel Joner, Velho Renata Voltolini, Pereira Jamile Queiroz, Corrêa Ana Paula Folmer, Brandelli Adriano

机构信息

Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves 9500, 91501-970 Porto Alegre, RS, Brazil.

出版信息

Enzyme Res. 2011;2011:487093. doi: 10.4061/2011/487093. Epub 2011 Oct 10.

DOI:10.4061/2011/487093
PMID:22007293
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3191812/
Abstract

A fungal isolate with capability to grow in keratinous substrate as only source of carbon and nitrogen was identified as Aspergillus niger using the sequencing of the ITS region of the rDNA. This strain produced a slightly acid keratinase and an acid protease during cultivation in feather meal. The peak of keratinolytic activity occurred in 48 h and the maximum proteolytic activity in 96 h. These enzymes were partly characterized as serine protease and aspartic protease, respectively. The effects of feather meal concentration and initial pH on enzyme production were evaluated using a central composite design combined with response surface methodology. The optimal conditions were determined as pH 5.0 for protease and 7.8 for keratinase and 20 g/L of feather meal, showing that both models were predictive. Production of keratinases by A. niger is a less-exploited field that might represent a novel and promising biotechnological application for this microorganism.

摘要

通过对rDNA的ITS区域进行测序，一株能够在角质底物作为唯一碳源和氮源的情况下生长的真菌分离株被鉴定为黑曲霉。该菌株在羽毛粉培养基中培养时产生了一种微酸性角蛋白酶和一种酸性蛋白酶。角蛋白分解活性在48小时达到峰值，蛋白水解活性在96小时达到最大值。这些酶分别部分被鉴定为丝氨酸蛋白酶和天冬氨酸蛋白酶。采用中心复合设计结合响应面法评估了羽毛粉浓度和初始pH对酶产生的影响。确定蛋白酶的最佳条件为pH 5.0，角蛋白酶为pH 7.8，羽毛粉浓度为20 g/L，表明这两种模型都具有预测性。黑曲霉产生角蛋白酶是一个较少被开发的领域，可能代表了这种微生物一种新的、有前景的生物技术应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/99a5bc166bff/ER2011-487093.006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/6fdf4f104aa3/ER2011-487093.001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/cfe459b68e64/ER2011-487093.002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/c83f1df042c4/ER2011-487093.003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/28145a812159/ER2011-487093.004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/30cbc5d637ec/ER2011-487093.005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/99a5bc166bff/ER2011-487093.006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/6fdf4f104aa3/ER2011-487093.001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/cfe459b68e64/ER2011-487093.002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/c83f1df042c4/ER2011-487093.003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/28145a812159/ER2011-487093.004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/30cbc5d637ec/ER2011-487093.005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de5/3191812/99a5bc166bff/ER2011-487093.006.jpg

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