Phosphate-mediated alteration of the Microsporum gypseum germination protease specificity for substrate: enhanced keratinase activity.

Abstract:

:Inorganic phosphate was found to decrease the caseinolytic and ethyl-esterase activities of the Microsporum gypseum germination protease. The germination protease possessed exokeratinase (beta-keratinase) activity immediately after release from the fungal spore. After phosphate treatment of the enzyme, the germination protease also possessed endo-keratinase (alpha-keratinase) activity. Phosphate altered the protease's pH optimum from 9.0 to 7.0 and decreased the molecular weight from 33,000 to 16,000. These values were identical to those found for the keratinase. Alpha- and beta-keratinase activities were stimulated in excess of 200-fold by disulfide reducing agents. Natural and suspected keratin degradation products also enhanced keratinase activity. Cell fractionation and in vitro conversion of the alkaline germination protease into a functional keratinase suggested that the subunits comprising the germination protease and the keratinase were of a common origin.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Page WJ,Stock JJ

doi

10.1128/JB.117.2.422-431.1974

subject

Has Abstract

pub_date

1974-02-01 00:00:00

pages

422-31

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

117

pub_type

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