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[Effect of certain substances on the biosynthesis of cellulase by the thermotolerant fungus, Aspergillus terreus I7P].

Different substrates which activate the enzyme synthesis were added to the natural medium for Asp. terreus 17P cultivation where wheat straw was used as the carbon source. Tween-80, oleic acid, sodium salts of ascorbic and acetic acid, potassium salt of indolyl acetic acid, sunflower seed oil, coreander seed oil, soapstock and sugars--glucose, sucrose, fructose and lactose were tested. An addition of Tween-80 at a concentration of 0.1% to the cultivation medium showed the most favourable effect on the synthesis of cellulolytic enzymes. Milk serum and cheese serum, malt shoots and protein-vitamin complex were examined as a substitute for corn extract. Dry malt shoots added at a concentration of 1.5% was a good substitute for corn extract.

Acetates↗
PubMed1998

[Subcloning and expression of coding region for cellulase binding domain of CBH I from P. janthinellum in E. coli].

The in vitro DNA manipulations, included the nested deletions, of cbh1 from P. janthinellum inserted into pUC18-181 were carried out. The two ends of fragments were modified into blunt ends and the fragments were self-ligated. Then, the encircled plasmids were transformed to E. coli JM109. Utilizing the characterization of CBD binding to crystalline cellulose, one catalytic domain deletion transformant producing active LacZ-CBD fusion protein was isolated from 24 transformants randomly picked from 400 transformants. The molecular weight of the LacZ-CBD fusion protein is 21 kD. The plasmid was designated pUC 18C. The LacZ-CBD fusion protein produced by JM109(pUC18C) was able to be purified by procedure of adsorption-desorption to cellulose. The pNPC activity of crude enzyme solution of JM109(pUC18C) induced by IPTG were zero, identified the JM109(pUC18C) has no CBHI activity.

Adsorption↗
PubMed1953

Cellulases.

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Cellulases↗