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Enhanced cellulase and β-glucosidase production by a mutant of Alternaria alternata

✍ Scribed by B. J. Macris


Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
232 KB
Volume
26
Category
Article
ISSN
0006-3592

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✦ Synopsis


Cellulose is the most abundant carbohydrate on this planet and its hydrolysis has been considered as a route towards its conversion into food, feeds, fuel, and chemicals. Enzymic hydrolysis of cellulose compares favorably to acid and alkali hydrolysis because enzymes are recoverable, specific, low in energy requirements, and nonpolluting. However, the cost of production and the low yield of cellulases are the major problems in the economics of the process and influence their application in a large-scale saccharification of cellulosic materials.' Among the thousands of microorganisms growing on cellulose as a sole carbon source, only a limited number of them excrete cellulases in the growth medium.2 Trichoderma spp. are the most intensively studied and favored microorganisms in this

The present work was undertaken to investigate the cellulolytic activity of the wild type and a mutant strain of A. alternata. This fungus has been previously reported to excrete a thermostable 6-D-galactosidase when grown in a whey liquid medium.8


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