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J Rogalski

Publications and source records attributed to J Rogalski.

5 recordsLinked to original sources

Cellulolytic activity of moulds. III. Enzymatic hydrolysis of cellulose by cellulase preparation from Aspergillus terreus F-413.

The strain Aspergillus terreus F-413 was used to obtain cellulolytic enzymes; it was cultivated on cellucotton by the submerged method in a 101 fermenter. The crude enzymatic preparation obtained from the post-culture liquid, containing small amounts of other enzymes besides active cellulases, was used for hydrolysis of several kinds of cellulose. The highest saccharification percentage was obtained with cellucotton and filter paper, while the lowest with lignocellulosic materials such as straw and sawdust. It was shown that cellulose pretreatment, both mechanical (grinding in a ball mill) and chemical (with alkali) distinctly increased the yield of enzymatic hydrolysis. In the obtained hydrolyzates the presence of glucose as the main product of cellulose decomposition was found.

Aspergillus

Cellulolytic activity of moulds. IV. Evaluation of the utility of cellulosic wastes for biosynthesis of cellulases and xylanase by Aspergillus terreus F-413.

The value of various cellulosic wastes for the synthesis of cellulolytic enzymes by the mould Aspergillus terreus F-413 was determined in submerged culture. The best results were obtained by using beet pulp. The dynamics of their synthesis was observed during a 12-day culture on the medium most favourable for the synthesis of cellulases.

Aspergillus

Cellulolytic activity of moulds. II. Various methods of precipitating and concentrating enzymes and their influence on the activity of cellulolytic preparation and xylanase of Aspergillus terreus F-413.

Complexes of cellulolytic enzymes and xylanase were precipitated and concentrated by various methods from post-culture liquids of Aspergillus terreus F-143, containing cellucotton as carbon source. The best results in regard to the specific activity of the preparations were obtained by precipitation of enzymes with acetone-denatured ethanol. Besides high cellulolytic and xylanase activity the crude enzyme preparation showed the presence of small amounts of amylase, protease and polygalacturonase.

Acetone

Isolation and properties of elongation factor 1 from Saccharomyces cerevisiae.

Polypeptide elongation factor 1 was isolated from yeast postribosomal supernatant. The highly purified factor was resolved on Ultrogel AcA-44 into two complementary fractions. One of these fractions contained two different polypeptide chains corresponding to a Ts-like elongation factor EF-1 beta gamma. The other fraction represented the light form of the factor, designated EF-1 alpha, with a molecular weight of approximately 50,000. The obtained results indicate that EF-1 from lower eukaryotes is also composed of three distinct polypeptides.

Fungal Proteins