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Title: Extracellular Production of a Novel Endo-β-Agarase AgaA from Pseudomonas vesicularis MA103 that Cleaves Agarose into Neoagarotetraose and Neoagarohexaose
Authors: Pang-Hung Hsu;Chien-Han Wei;Wen-Jung Lu;Fen Shen;Chorng-Liang Pan;Hong-Ting Victor Lin
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: agar;agarase;neoagaro-oligosaccharides;Pseudomonas vesicularis;osmotic shock;extracellular
Date: 2015
Issue Date: 2017-07-31T01:47:33Z
Publisher: International Journal of Molecular Sciences
Abstract: Abstract:The gene agaA, of the isolated marine bacterium Pseudomonas vesicularis MA103, comprised 2958-bp nucleotides encoding a putative agarase AgaA of 985 amino acids, which was predicted to contain a signal peptide of 29 amino acids in the N-terminus, a catalytic domain of glycoside hydrolase 16 (GH16) family, a bacterial immunoglobulin group 2 (Big 2), and three carbohydrate binding modules 6 (CBM 6). The gene agaA was cloned and overexpressed in Escherichia coli, and the optimum temperatures for AgaA overexpression were 16, 20 and 24 °C. The agaA was cloned without its signal peptide for cytosolic production overexpression, whereas it was cloned with the heterologous signal peptide PelB and its endogenous signal peptide for periplasmic and extracellular productions, respectively. Extracellular and periplasmic rAgaA showed greater activity than that of cytosolic rAgaA, indicating that membrane translocation of AgaA may encourage proper protein folding. Time-course hydrolysis of agarose by rAgaA was accomplished and the products were analyzed using thin layer chromatography and matrix-assisted laser desorption inoization-time of flight mass spectrometry, indicating that AgaA from P. vesicularis was an endo-type β-1,4 agarase that cleaved agarose into neoagarotetraose and neoagarohexaose as the final products.
Relation: 16(3), pp.5590-5603
Appears in Collections:[Department of Food Science] Periodical Articles

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