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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39226

Title: Purification and characterization of Aeromonas salmonicida MAEF108 agarase AS-II
Authors: Shao-Chi Wu;Sheen-Kye Kang;Chorng-Liang Pan
Contributors: 國立臺灣海洋大學:食品科學系
Date: 2012
Issue Date: 2016-11-28T08:33:26Z
Publisher: Journal of the Fisheries Society of Taiwan
Abstract: ABSTRACT: Agarase AS-II was purified from the four fractions having agarase activities of marine bacteria Aeromonas (A.) salmonicida MAEF108 crude agarases. The culture suspension of A. salmonicida MAEF108 was centrifuged, ultrafiltrated, then applied to DE-52 ion-exchange chromatography to obtain Agarase AS-II, which was 44.03 fold after purification and estimated as a 95.4 kDa single protein. The optimum temperature and pH for the 0.2% agarose degrading activity of Agarase AS-II was 45°C and 7.0. Agarase AS-II maintained 60% residual activity when stored below 40oC for 2 h; the stability of Agarase AS-II was optimal in pH 6.0-8.0 phosphate buffer. The addition of 5 mM CaCl2 in assay buffer contributed 30% higher relative activity than when no metal ions were added. The activation energy and Km of Agarase AS-II was 46.24 J mol-1K-1 and 4.39% of agarose, respectively. The Agarase AS-II had substrate specificity on Rhodophyta and its refined products. It could degrade the substrate to final products, such as neoagarohexaose (N6) and neoagarotetraose (N4), indicating Agarase AS-II could be regarded as a β-agarase, which would directly degrade agarose to produce N6 and N4. In addition, Agarase AS-II has the abilities to biosynthesize N4 and galactose oligomers from neoagarobiose (N2) and galactose, respectively.
Relation: 39(1)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39226
Appears in Collections:[食品科學系] 期刊論文

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