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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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Published in: | Applied biochemistry and biotechnology 2006-05, Vol.133 (2), p.163-170 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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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. |
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ISSN: | 0273-2289 1559-0291 |
DOI: | 10.1385/ABAB:133:2:163 |