Abstract
We aimed in the current study, the identification of a marine bacterial amylase produced by Bacillus pacificus, which was associated with Turbinaria ornata. Cultural conditions were optimized for the highest amylase production on Tryptic soy broth media supplemented with starch 1% at initial pH 9, 55 °C for 24 h. The newly purified amylase was characterized for a possible biotechnological application. Data indicated that the obtained amylase with a molecular weight of 40 kD and the N-terminal sequence of the first 30 amino acids of amBp showed a high degree of homology with known alpha amylase, and was stable at 60 °C of pH 11. Among the tested substrate analogs, amBp was almost fully active on Alylose and Alylopectine (97%), but moderately hydrolyzed glycogen < sucrose < maltose < lactose. Therefore, the current amylase mainly generated maltohexaose from starch. Mg2+ and Zn2+ improved amylase activity up to 170%. While ethylenediamine tetraacetic acid (EDTA) similarly induced the greatest activity with purified amylase, PCMB had the least effect. Regarding all these characteristics, amylase from marine bacterial symbionts amBp has a new promising feature for probable therapeutic, industrial, and nutritional applications.
Highlights
Starch is a glucose polymer containing of two types of α-glucans, amylose and amylopectin, Amylose is a linear water insoluble polymer of glucose joined by α-1, 4 glycosidic bonds, while amylopectin is branched water soluble polysaccharide with short α-1, 4 and α-1, 6 [1]
Our findings demonstrated that the Optimizationhighest of theα-amylase detected activity marine
Bacterial strains associated with the brown alga Turbinaria ornata were isolated from the surface of the macroalga collected from shallow surface of the
Summary
Starch is a glucose polymer containing of two types of α-glucans, amylose and amylopectin, Amylose is a linear water insoluble polymer of glucose joined by α-1, 4 glycosidic bonds, while amylopectin is branched water soluble polysaccharide with short α-1, 4 and α-1, 6 [1]. Based on the mode of action, starch hydrolyzing enzymes may be endo-acting or exo-acting. Α-Amylases (EC 3.2.1.1), categorized in GH-13 family of glyosyl hydrolases, are the extracellular endo-acting enzymes that hydrolyse α-1,4 glycosidic linkages of starch randomly, while bypassing the branch points and liberating α-limit dextrins as products [2], Sivaram, 1993 #271. Amylases are universally distributed throughout the animal, plant, and microbial [4]. Despite the large difference in the characteristics of microbial α-amylases, their molecular weights are generally in the same range of 40 to 70 kDa [1]. It has been reported that the α-amylase from Chloroflexus aurantiacus have the highest molecular weight with 210 licenses/by/4.0/)
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