Secreted fungal aspartic proteases: A review.

Virginia Mandujano-González, Lourdes Villa-Tanaca, Miguel Angel Anducho-Reyes, Yuridia Mercado-Flores

Journal: Revista iberoamericana de micologia 2017;33(2):76-82

PMID: 27137097

Full Text on Elsevier Science View on PubMed

Abstract

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.

Address: Universidad Politécnica de Pachuca, Zempoala, Hidalgo, Mexico.; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Mexico City, Mexico.; Universidad Politécnica de Pachuca, Zempoala, Hidalgo, Mexico. Electronic address: [email protected].

DOI: 10.1016/j.riam.2015.10.003

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MeSH Terms: Amino Acid Motifs, Aspartic Acid Proteases, Catalytic Domain, Enzyme Precursors, Food Microbiology, Fungal Proteins, Fungi, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Hydrogen-Ion Concentration, Industrial Microbiology, Protease Inhibitors, Substrate Specificity