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Inducible character of β‐xylanase in a hyperproducing mutant of Thermomyces lanuginosus
Author(s) -
Santhosh Kumar Kuttanpillai,
Permaul Kugen,
Singh Suren
Publication year - 2009
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.200900017
Subject(s) - xylanase , xylobiose , xylan , xylose , inducer , chemistry , biochemistry , mutant , polysaccharide , strain (injury) , mutagenesis , enzyme , biology , fermentation , anatomy , gene
Abstract Ten strains of Thermomyces lanuginosus from various culture collections were evaluated for extracellular endo‐ β ‐1,4‐xylanase production. The best xylanase producer (5771±173 nkat/mL) T. lanuginosus SK, was subjected to UV and N ‐methyl‐ N ‐nitro‐ N ‐nitrosoguanidine mutagenesis. A mutant strain T. lanuginosus MC134, that showed on oatspelts xylan a 1.5 fold higher xylanase production than the parent strain SK, was subjected to a study of the regulation of xylanase synthesis during growth on various carbohydrates and during induction in glucose‐grown cells. In the growth experiments the highest production of xylanase was observed in the presence of xylans, however, an appreciable amount of the enzyme, about 10%, was also produced during growth on xylose. Xylobiose was found to be the most efficient xylanase inducer in the glucose‐grown cells. Its induction efficiency was followed by xylose, beechwood and birchwood xylan. Xylanase induction by polysaccharides started several hours later but proceeded for a longer time than that induced by the low molecular mass inducers, indicating that the polysaccharides serve as more sustainable source of inducers and that they have to be first hydrolyzed by the low level of constitutively synthesized xylanase. The repression of the induction of xylanase by glucose confirmed that the xylanase synthesis in the mutant strain is similar to the parent strain and exhibits an induction‐repression regulation mechanism.

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