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Production of b-galactosidase by Trichoderma reesei FTKO-39 in wheat bran. Partial Purification of two Isozymes

Trichoderma reesei FTKO-39 grown at 35C for 5 d on wheat bran supplemented with MgCl sub(2) and lactose as the carbon source produced two isozymes of b-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimu...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 2006-05, Vol.133 (2), p.163-170
Main Authors: Adalberto, PR, Massabni, A C, Goulart, A J, Contiero, J, Carmona, E C, Cardello, L, Monti, R
Format: Article
Language:English
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Summary:Trichoderma reesei FTKO-39 grown at 35C for 5 d on wheat bran supplemented with MgCl sub(2) and lactose as the carbon source produced two isozymes of b-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimum activity at 65C, but the pH optima were 4.0 and 6.5, respectively. The isozymes also showed similar thermal stability. However, BGT I was more stable than BGT II in a pH range of 3.0-10.0. At least two different b-galactosidases are produced by T. reesei, as revealed by the two bands seen on a 6% polyacrylamide gel stained for activity.
ISSN:0273-2289
1559-0291
DOI:10.1385/ABAB:133:2:163