Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius.

Anjana Devi, N and Appu Rao, A. G. (1996) Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius. Enzyme and Microbial Technology, 18 (1). 59-65, 19 ref..

PDF Enzyme_&_Microbial_Technology_18(1)_1996_59-65.pdf Restricted to Registered users only Download (721kB)

Abstract

Multiple forms of polygalacturonases [EC 3.2.1.15] are produced by Aspergillus carbonarius. 3 forms of this enzyme, differing in mol. wt. (PG I, 61 000; PG II, 42 000; and PG III, 47 000 Da) and enzymic properties, were isolated and purified to apparent homogeneity by molecular sieve chromatography on Sephacryl S-200, ion exchange chromatography on CM Sephadex and gel filtration on Sephadex G-50 superfine. All 3 enzymes are endo-enzymes with high affinity for polygalacturonic acid. One of the forms, PG II, which accounts for >60% of total polygalacturonase activity, had a high specific activity (7000 U mg-1 protein). The 3 enzymes differed in their amino acid composition, substrate affinity, sensitivity toward metal ions and thermal stability. The midpoint of thermal inactivation temp. (Tm) was 43, 46 and 54C for PG I, PG II and PG III, respectively. Thermal inactivation of the multiple forms followed 1st-order kinetics with estimated half-lives of 6, 10 and 32 min, respectively.

Item Type:	Article
Uncontrolled Keywords:	ASPERGILLUS-; ENZYMES-; FUNGI-; GLYCOSIDASES-; PECTIC-ENZYMES; POLYGALACTURONASES-
Subjects:	500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 28 Polysaccharide Chemistry
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	26 Nov 2008 11:00
Last Modified:	28 Dec 2011 10:01
URI:	http://ir.cftri.res.in/id/eprint/7859

Actions (login required)

View Item