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Glucoamylase of Aspergillus niger.

IR@CSIR-CFTRI

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Relation http://ir.cftri.com/4291/
 
Title Glucoamylase of Aspergillus niger.
 
Creator Venkataramu, K.
Manjunath, P.
Raghavendra Rao, M. R.
 
Subject 04 Fungi
05 Enzymes
 
Description 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.
 
Date 1975
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/4291/1/Indian%20Journal%20of%20Biochemistry%20and%20Biophysics%2C%20Volume-12%28%20%281975%29%20107-114.pdf
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.