Secreted fungal aspartic proteases: A review

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• 作者：Virginia Mandujano-Gonzá ; lez^a ; Lourdes Villa-Tanaca^b ; Miguel Angel Anducho-Reyes^a ; Yuridia Mercado-Flores^a ; ^{yuridiamercado@upp.edu.mx" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Secreted aspartic proteases ; Fungal enzymes ; E.C.3.4.23
• 刊名：Revista Iberoamericana de Micología
• 出版年：2016
• 出版时间：April-June 2016
• 年：2016
• 卷：33
• 期：2
• 页码：76-82
• 全文大小：1345 K

文摘

The aspartic proteases, also called aspartyl and aspartate proteases or acid proteases (E.C.3.4.23), belong to the endopeptidase family and are characterized by the conserved sequence Asp-Gly-Thr at the active site. These enzymes are found in a wide variety of microorganisms in which they perform important functions related to nutrition and pathogenesis. In addition, their high activity and stability at acid pH make them attractive for industrial application in the food industry; specifically, they are used as milk-coagulating agents in cheese production or serve to improve the taste of some foods. This review presents an analysis of the characteristics and properties of secreted microbial aspartic proteases and their potential for commercial application.