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Enteromorpha polysaccharides (EP) extracted from green algae have displayed a wide varietyof biological activities. However, their high molecular weight leads to a high viscosity and lowsolubility, and therefore, greatly restrains their application. To solve this problem, bacteriafrom the surface of Enteromorpha were screened, and an Alteromonas macleodii strain B7 wasfound to be able to decrease the molecular weight of EP in culture media. Proteins harvestedfrom the supernatant of the A. macleodii B7 culture were subjected to native gel electrophoresis,and a band corresponding to the Enteromorpha polysaccharide lyase (EPL) was detected byactivity staining. The enzyme identity was subsequently confirmed by MALDI-TOF/TOFmass spectrometry as the putative α-amylase reported in A. macleodii ATCC 27126. Theamylase gene (amySTU) from A. macleodii B7 was cloned into Escherichia coli, resulting in highlevelexpression of the recombinant enzyme with EP-degrading activity. AmySTU was foundto be cold-adapted; however, its optimal enzyme activity was detected at 40oC. The α-amylasewas highly stable over a broad pH range (5.5-10) with the optimal pH at 7.5-8.0. The highestenzyme activity was detected when NaCl concentration was 2%, which dropped by 50% whenthe NaCl concentration was increased to 16%, showing an excellent nature of halotolerance. Furthermore, the amylase activity was not significantly affected by tested surfactants or thepresence of some organic solvents. Therefore, the A. macleodii strain B7 and its α-amylase canbe useful in lowering EP molecular weight and in starch processing.

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