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Purification and characterization of glucoamylase from a higher yielding mutant of Aspergillus candidus Link var. aureus

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Summary

A higher yielding mutant of Aspergillus candidus Link var. aureus has been isolated using the chemical mutagen N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) at 5 μg/ml concentration of the mutagen. This mutant produces 88 to 111 U/ml of glucoamylase compared with 40 to 50 U/ml produced by the parent strain. The enzyme from this mutant has been purified to homogeneity using hydrophobic interaction chromatography and a DEAE-cellulose column with over 65% recovery of the enzyme activity and 21-fold purification. The mutant protein is very similar to the enzyme from the parent strain in that it cochromatographs with the parent enzyme on phenylglycyl-Sepharose, norleucyl-Sepharose, Sepharose-CL-6B, Concanavalin A-Sepharose, DEAE-cellulose and DEAE-Sephadex-A-50. The two proteins exhibit similar electrophoretic behavior and have similar molecular weights and amino acid composition. However, the specific activity of the purified mutant protein is 1125 U/mg compared with 560 U/mg for the parent enzyme. Further genetic analysis of the mutant is needed to explain these observations.

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Kolhekar, S.R., Mahajan, P.B., Ambedkar, S.S. et al. Purification and characterization of glucoamylase from a higher yielding mutant of Aspergillus candidus Link var. aureus . Appl Microbiol Biotechnol 22, 181–186 (1985). https://doi.org/10.1007/BF00253606

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  • DOI: https://doi.org/10.1007/BF00253606

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