Secreted fungal aspartic proteases: A review

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

doi:10.1016/j.riam.2015.10.003

Secreted fungal aspartic proteases: A review

Título traducido de la contribución: Aspartil-proteasas secretadas por hongos: revisión

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

Escuela Nacional de Ciencias Biológicas (ENCB)

Producción científica: Contribución a una revista › Estudio breve › revisión exhaustiva

68 Citas (Scopus)

Resumen

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.

Título traducido de la contribución	Aspartil-proteasas secretadas por hongos: revisión
Idioma original	Inglés
Páginas (desde-hasta)	76-82
Número de páginas	7
Publicación	Revista Iberoamericana de Micologia
Volumen	33
N.º	2
DOI	https://doi.org/10.1016/j.riam.2015.10.003
Estado	Publicada - 1 abr. 2016

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10.1016/j.riam.2015.10.003

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title = "Secreted fungal aspartic proteases: A review",

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.",

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AU - Villa-Tanaca, Lourdes

AU - Anducho-Reyes, Miguel Angel

AU - Mercado-Flores, Yuridia

PY - 2016/4/1

Y1 - 2016/4/1

N2 - 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.

AB - 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.

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DO - 10.1016/j.riam.2015.10.003

M3 - Estudio breve

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JO - Revista Iberoamericana de Micologia

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Secreted fungal aspartic proteases: A review

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