[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Studies on the two forms of amyloglucosidase of Aspergillus niger van Tieghem.

Ramasesh, N. and Sreekantiah, K. R. and Murthy, V. S. (1982) Studies on the two forms of amyloglucosidase of Aspergillus niger van Tieghem. Starch/Staerke, 34 (10). 346-351, 26 ref..

[img] PDF
starchstarke 34 (1982) Nr. 10, S. 346-351.pdf - Published Version
Restricted to Registered users only

Download (578kB)

Abstract

2 isoenzymes of amyloglucosidase, designated as AG-I and AG-II, elaborated exocellularly by a strain of Aspergillus niger van Tieghem, were separated and purified to homogeneity. The enzymes, produced in a selective medium, were separated and purified on a column of DEAE-Sephadex A-50. The mol. wt. of AG-I and AG-II were 69 810 and 89 130, resp. The 2 enzymes were glycoproteins and differed in their carbohydrate contents, pH and temp. stabilities and optima for activity. Their activation energies and Km values also varied. AG-II, had a higher mol. wt., carbohydrate content, increased acid tolerance and was synthesized earlier than AG-I (when the pH of the medium was acid). Hg and Ag salts caused partial inhibition of their activities.

Item Type: Article
Uncontrolled Keywords: GLUCOSIDASES-; Aspergillus niger, amyloglucosidases isoenzymes characteristics from; ASPERGILLUS-; amyloglucosidases isoenzymes characteristics from Aspergillus niger
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 25 May 2016 06:45
Last Modified: 25 May 2016 06:45
URI: http://ir.cftri.res.in/id/eprint/6767

Actions (login required)

View Item View Item