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Qualitative and quantitative changes in β‐1,4‐glucosidase accompanying growth of Aspergillus nidulans
Author(s) -
Sharma S.,
Bagga P. S.,
Sandhu D. K.
Publication year - 1990
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620300513
Subject(s) - aspergillus nidulans , spore , hypha , mutant , strain (injury) , isozyme , conidium , biology , wild type , enzyme , somatic cell , biochemistry , chemistry , microbiology and biotechnology , botany , gene , anatomy
A comparative study of the wild type A. nidulans and a mutant strain aco‐T69 (lacking conidia and cleistothecia) revealed the better production of β‐1,4‐glucosidase in the former. The relative distribution of the enzyme levels in various morphological structures viz. somatic hyphae, spores and cleistothecia also showed a variation. Highest specific activity was found in the cleistothecial extracts. The electrophoretic analysis of the wild type strain demonstrated the presence of three isoenzymes of β‐1,4‐glucosidase i.e. β‐GLU I, β‐GLU II and β‐GLU III, the number of which varies from one to three during the growth of the organism. The parallel study of the mutant strain showed complete absence of β‐GLU II. All three forms were present in the somatic hyphae and cleistothecial extracts while spore extracts depicted the absence of β‐GLU III in the wild type.