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Digestion of residual beta-cyclodextrin in treated egg using glucoamylase from a mutant strain of Aspergillus niger (CFTRI 1105)

Rao, P; Suresh, C; Rao, DN; Kumar, SU; Divakar, S
Glucoamylase enzyme isolated from the cultures of a mutant strain of Aspergillus niger (CFTRI 1105) was found to digest beta-cyclodextrin in standard 1% solutions as well as in beta-cyclodextrin-treated egg yolk and whole egg samples. About 70-95% of beta-cyclodextrin in samples was digested with both dilute (reducing sugar activity 870 units) and concentrated (34,800 units) enzyme solutions at 40 degrees C and 70 degrees C for incubation periods of 15-360 min. (C) 1999 Elsevier Science Ltd. All rights reserved.
ISI:000079211200003
ISSN: 0308-8146
CID: 2507582

Characterisation of a starch-hydrolysing enzyme of Aspergillus niger

Suresh, C; Dubey, A K; Srikanta, S; Kumar, S U; Karanth, N G
A UV-induced mutant strain of Aspergillus niger (CFTRI-1105-U9) overproduced a starch-hydrolysing enzyme with properties characteristically different from the known amylases of the fungus. The purified enzyme of 4.0 pI had an apparent molecular mass of 125 kDa and it dextrinised starch and then saccharified the dextrins. Patterns of the enzyme activity on starch, resulting in glucose at 60 degrees C and glucose, maltose and maltodextrins at 70 degrees C as primary products, suggested significant applications for the enzyme in starch-processing industries.
PMID: 10390823
ISSN: 0175-7598
CID: 2507532

Separation and direct detection of raw and gelatinized starch hydrolyzing activities of glucoamylase on isoelectric focusing gels

Suresh, C; Dubey, A K; Kini, R; Umesh-Kumar, S; Karanth, N G
A procedure to detect raw and gelatinized starch activities of glucoamylase on isoelectric focusing (IEF) gels by using 2, 3, 5-triphenyltetrazolium chloride is described. The reagent reacts with the reducing group of glucose released by glucoamylase from the substrate starch. Using the reaction, production of glucoamylase by Aspergillus niger was detected on 10% IEF gels within a pH range of 2.5-9.5. Since the method can detect raw and gelatinized starch activities of glucomylase associated with 1 microg protein, it will be useful for enzyme engineering studies that involve screening of various mutations.
PMID: 10217158
ISSN: 0173-0835
CID: 2507542

An immunoaffinity procedure for determination of enzyme activity at elevated temperatures

Suresh, C; Dubey, A K; Kavitha, R; Umesh-Kumar, S
PMID: 9866696
ISSN: 0003-2697
CID: 2507512

An enzyme-linked immunosorbent assay for the estimation of fungal biomass during solid-state fermentation

Dubey, A K; Suresh, C; Kumar, S U; Karanth, N G
An enzyme-linked immunosorbent assay for sensitive, specific and quantitative estimation of fungal biomass during solid-state fermentation is described. Using this method, differential growth rates and colonization of the substrate can be studied. The assay has potential application for the efficient monitoring of solid-state fermentation involving specific fungus, for which available methods are not adequate.
PMID: 9802214
ISSN: 0175-7598
CID: 2507552