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Biochem Soc Trans. 2004 Apr;32(Pt 2):276-8.

Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles.

Author information

1
Department of Microbiology, University of Delhi South Campus, New Delhi-110021, India. tsnarayana@vsnl.net

Abstract

The extensive efforts to screen thermophilic fungi and bacteria, isolated from various environmental samples, have resulted in the selection of Thermomucor indicae-seudaticae, Geobacillus thermoleovorans NP33 and G. thermoleovorans NP54 for the production of glucoamylase, amylopullulanase and alpha-amylase, respectively. Submerged and solid-state fermentation processes were optimized for maximizing the secretion of glucoamylase by T. indicae-seudaticae. The production of amylopullulanase and alpha-amylase by NP33 and NP54 in submerged fermentation was also optimized. Glucoamylase was optimally active at pH 7.0 and 60 degrees C and was shown to saccharify soluble as well as raw starches. Amylopullulanase and alpha-amylase exhibited optima at pH 7.0 and 100 degrees C and saccharified starch efficiently. Differential inhibition and action on mixed substrates clearly suggested that there are two separate active sites for alpha-amylase and pullulanase activities of amylopullulanase. Both alpha-amylase and amylopullulanase are high maltose-forming and Ca(2+)-independent. These amylolytic enzymes have been shown to be useful in starch saccharification alone and in combination.

PMID:
15046588
DOI:
10.1042/bst0320276
[Indexed for MEDLINE]

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