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Molecules 2015, 20(2), 1955-1967;

Purification and Characterization of Chitinases from Ridgetail White Prawn Exopalaemon carinicauda

Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
University of Chinese Academy of Sciences, Beijing 100039, China
Author to whom correspondence should be addressed.
Academic Editor: Vito Ferro
Received: 17 December 2014 / Accepted: 19 January 2015 / Published: 26 January 2015
(This article belongs to the Collection Advances in Carbohydrate Chemistry)
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In this paper, we purified two native chitinases from the hepatopancreas of the ridgetail white prawn Exopalaemon carinicauda by using ion-exchange resin chromatography (IEC) and gel filtration. These two chitinases, named EcChi1 and EcChi2, were identified by chitinolytic activity assay and LC-ESI-MS/MS. Their apparent molecular weights were 44 kDa and 65 kDa as determined by sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The specific activity of EcChi1 and EcChi2 was 1305.97 U·mg−1 and 28.69 U·mg−1. The optimal temperature and pH of EcChi1 were 37 °C and pH 4.0, respectively. Co2+, Fe3+, Zn2+, Cd2+, and Cu2+ had an obvious promoting effect upon chitinase activity of EcChi1. For colloidal chitin, the Km and Vmax values of EcChi1 were 2.09 mg·mL−1 and 31.15 U·mL−1·h−1. View Full-Text
Keywords: chitinase; enzymatic characterization; Exopalaemon carinicauda chitinase; enzymatic characterization; Exopalaemon carinicauda

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Wang, J.; Zhang, J.; Song, F.; Gui, T.; Xiang, J. Purification and Characterization of Chitinases from Ridgetail White Prawn Exopalaemon carinicauda. Molecules 2015, 20, 1955-1967.

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