2 research outputs found
<span style="font-size:15.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI;mso-bidi-font-weight:bold" lang="EN-GB">Study on calcium ion independent α-amylase from haloalkaliphilic marine <i>Streptomyces</i><span style="mso-bidi-font-style: italic"> strain A3</span></span>
427-437In the present investigation,
authors have reported novel calcium ion independent α-amylase enzyme from less
extensively studied marine Streptomyces strain A3. The isolated strain
was identified on the basis of 16S rDNA sequencing and scanning electron
microscopy. The α-amylase from strain A3 was purified to homogeneity with the
aid of ammonium sulfate precipitation and gel filtration chromatography by
using Sephadex G-75, insoluble corn starch and sephacryl
S-100 column, with a 43.92-fold increase in specific activity. SDS-PAGE and
zymogram activity staining showed a single band equal to molecular mass of 45
kDa. The activity and stability of enzyme didn’t increase in presence of
calcium ion, indicating calcium ion independent nature of amylase. Enzyme
retained considerable activity in presence of oxidants and commercial
detergents. Glucose, maltose and maltotriose were the main end product of
starch hydrolysis, indicating that enzyme is an <span style="mso-bidi-font-weight:
bold">α-amylase. Therefore, it can be concluded that the surfactant,
detergent stable and calcium ion independent
α-amylase from strain A3 has widespread applications for detergent and
pharmaceutical industry where higher salt concentration inhibits enzymatic
conversion. In addition to that, application of this amylase may eliminate the
use of calcium in starch liquefaction and subsequent removal by ion exchange.
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