The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260
CHARACTERIZATION OF EXTRACELLULAR PROTEINASES OF THE GENUS MONASCUS BY THEIR pH-ACTIVITY PROFILES
JIRO NISHIKAWAYAEKO WATANABEJUN KASHIMURAKEIICHI ASOHIROSHI IIZUKA
Author information
JOURNAL FREE ACCESS

1988 Volume 34 Issue 6 Pages 467-473

Details
Abstract
Extracellular proteinase activities produced by 36 strains in the genus Monascus were determined at various pHs using casein and Azocoll as substrates. These strains were grouped into three types (A, B, and C) according to the pH-activity profiles of their proteinases.
Type A was characterized by only acid proteinases with an optimal pH around 3 and was found in eight strains of six species of Monascus (i.e., M. araneosus, M. fuliginosus, M. kaoliang, M. pilosus, M. pubigerus, and M. vitreus). Type B was characterized by only alkaline proteinases with an optimal pH about 8-9 and was found in 24 strains of nine species and two varieties of Monascus (i.e., M. albidus, M. albidus var. glaber, M. anka, M. anka var. rubellus, M. araneosus, M. kaoliang, M. major, M. purpureus, M. ruber, M. rubiginosus, and M. serorubescens). Type C was characterized by the two kinds of proteinases observed in types A and B and was found in three strains of one species of Monascus (i.e., M. kaoliang).
It was revealed in this study that Monascus spp. secreted extracellular alkaline proteinases. However, there was not any considerable correlation between the classification system of the genus Monascus and the type of proteinase produced.
Content from these authors
© The Microbiology Research Foundation
Previous article Next article
feedback
Top