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Glucoamylase of Aspergillus niger.

Venkataramu, K. and Manjunath, P. and Raghavendra Rao, M. R. (1975) Glucoamylase of Aspergillus niger. Indian Journal of Biochemistry and Biophysics, 12. pp. 107-114.

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Abstract

Three glucoamylases (A, B and C) from Aspergilhs niger NRRL 330 have been isolated in homogeneous state (75%) by ethanol fractionation and DEAE-cellulose chromatography. The major fraction (B) has a specific activity of 38. The temperature and pH optirna for these glucoamylases are in the ranges of 50.(10° and 3.5-4.5 respectively. A is most and C is least stable at 60°. They (A, B and C) are all glycoproteins containing 8.2, 18 and 6.2% carbohydrate respectively. The extent of lnactivation of the enzymes by periodate depends upoo oxidant concentration and the period of treatment. Photooxidation in the presence of 0.01%of either methylene blue or Rose Bengal results in partial loss of activity at pH 8.9 but none at pH 5. Diisopropylfloorophosphate, p-ehloromercuribenzoate, N-ethylrnaleinlide, iodoaciJtate and N-bromosuccinimidc (all at 2 mm for 30 min) have no effect on the glucoanwL1ses. The enzymes are fully active in 8 M urea, but 2 M guanidine hydrochloride abolished reversibly all activity. Gel filtration and 5DS-polyacrylamide electrophoresis gave molecnlar weights of 80,000 to 90,000 for A, and abont 70,000 for Band C. All of them seem to possess phenylalanine and leucinefisoleucine at the N- and C-terminal ends respectively. Many of these properties make them distinct from the glucoamylases described by Pazur and by Lineback.

Item Type: Article
Uncontrolled Keywords: Aspergillus niger NRRL 330, glucoamylases
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology > 04 Fungi
600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Jul 2016 07:25
Last Modified: 14 Jul 2016 07:25
URI: http://ir.cftri.com/id/eprint/4291

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