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Study of β‐1,3‐glucanase activity during autolysis of Aspergillus nidulans by FPLC ion‐exchange chromatography
Author(s) -
Nuero O. M.,
Alfonso C.,
Amo F. Del,
Reyes F.
Publication year - 1993
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1993.tb01435.x
Subject(s) - autolysis (biology) , glucanase , fast protein liquid chromatography , aspergillus nidulans , biology , biochemistry , pectin , chemistry , enzyme , mutant , gene
The behaviour of β‐1,3‐glucanase activity during Aspergillus nidulans autolysis was studied in a basal medium and in the same medium supplemented with 0.5 g l ‐1 of microcrystalline cellulose, laminarin, pectin, seedling of Lycopersicum esculentum extract, chitin and xylan respectively. In any case β‐1,3‐glucanase activity was detected in the culture fluid before the onset of the autolysis, but afterwards a progressive increase of β‐1,3‐glucanase activity took place with incubation time. In the media supplemented with pectin and seedling of Lycopersicum esculentum extract higher activity in the first days of autolysis was found. The activity at the end of the studied process by sample was 2.5, 2.1, 2.5, 1.9, 2.2, 2.3 and 2.3 U, and the specific activity 83, 53, 85, 55, 64, 90 and 53 mU mg ‐1 of protein for each medium respectively. The β‐1,3‐glucanase activity in Aspergillus nidulans seems to be related to autolysis and not to the presence of different substances in the culture medium. The behaviour of β‐1,3‐glucanase activity during the degradative process was followed by FPLC ion‐exchange chromatography. Three proteins (I, II, III) with β‐1,3‐glucanase activity were separated and quantified. These proteins have similar behaviour in all the media. Proteins I and II increase progressively with incubation time but protein III is only present at the first and last days of autolysis.