<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. </span