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

Translated title of the contribution: Secreted fungal aspartic proteases: A review

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

Escuela Nacional de Ciencias Biológicas (ENCB)

Research output: Contribution to journal › Short survey › peer-review

68 Scopus citations

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.

Translated title of the contribution	Secreted fungal aspartic proteases: A review
Original language	English
Pages (from-to)	76-82
Number of pages	7
Journal	Revista Iberoamericana de Micologia
Volume	33
Issue number	2
DOIs	https://doi.org/10.1016/j.riam.2015.10.003
State	Published - 1 Apr 2016

Keywords

E.C.3.4.23
Fungal enzymes
Secreted aspartic proteases

Access to Document

10.1016/j.riam.2015.10.003

Cite this

@article{a431719cc6ba4b44993f22e590d4e5fb,

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.",

keywords = "E.C.3.4.23, Fungal enzymes, Secreted aspartic proteases",

author = "Virginia Mandujano-Gonz{\'a}lez and Lourdes Villa-Tanaca and Anducho-Reyes, {Miguel Angel} and Yuridia Mercado-Flores",

note = "Publisher Copyright: {\textcopyright} 2016 Asociaci{\'o}n Espa{\~n}ola de Micolog{\'i}a",

year = "2016",

month = apr,

day = "1",

doi = "10.1016/j.riam.2015.10.003",

language = "Ingl{\'e}s",

volume = "33",

pages = "76--82",

journal = "Revista Iberoamericana de Micologia",

issn = "1130-1406",

number = "2",

}

TY - JOUR

T1 - Secreted fungal aspartic proteases

T2 - A review

AU - Mandujano-González, Virginia

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.

KW - E.C.3.4.23

KW - Fungal enzymes

KW - Secreted aspartic proteases

UR - http://www.scopus.com/inward/record.url?scp=84964584132&partnerID=8YFLogxK

U2 - 10.1016/j.riam.2015.10.003

DO - 10.1016/j.riam.2015.10.003

M3 - Estudio breve

SN - 1130-1406

VL - 33

SP - 76

EP - 82

JO - Revista Iberoamericana de Micologia

JF - Revista Iberoamericana de Micologia

IS - 2

ER -

Secreted fungal aspartic proteases: A review

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this