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Finore Ilaria Kasavi Ceyda Poli Annarita Romano Ida Oner Ebru Toksoy Kirdar Betul Dipasquale Laura Nicolaus Barbara Lama Licia 《World journal of microbiology & biotechnology》2011,27(10):2425-2433
This study reports the purification and biochemical characterization of a raw starch-digesting α-amylase from Geobacillus thermoleovorans subsp. stromboliensis subsp. nov. (strain PizzoT). The molecular weight was estimated to be 58 kDa by SDS–PAGE. The enzyme was highly active over a wide range of pH from
4.0–10.0. The optimum temperature of the enzyme was 70°C. It showed extreme thermostability in the presence of Ca2+, retaining 50% of its initial activity after 90 h at 70°C. The enzyme efficiently hydrolyzed 20% (w/v) of raw starches, concentration
normally used in starch industries. The α-amylase showed an high stability in presence of many organic solvents. In particular
the residual activity was of 73% in presence of 15% (v/v) ethyl alcohol, which corresponds to ethanol yield in yeast fermentation
process. By analyzing its complete amyA gene sequence (1,542 bp), the enzyme was proposed to be a new α-amylase. 相似文献
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