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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Review Article

Physicochemical properties and behavior in solution of three cellulases from haliotis fulgens

Author(s): Alejandra Hernandez-Santoyo, Arturo Rojo-Domfnguez, Enrique Garcfa-Hernandez and Adela Rodrfguez-Romero*

Volume 7, Issue 6, 2000

Page: [389 - 396] Pages: 8

DOI: 10.2174/092986650706221207163656

Price: $65

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Abstract

Three proteins that showed activity over cellulosic substrates were isolated from the hepatopancreas of the blue abalone Haliotis fulgens. The purified cellulases are acidic with molecular weights between 17 900 and 30 300. Activity experiments indicated that they are endo-, exo- and l3-glucanases. These proteins form large aggregates as demonstrated by means of DLS experiments, which can be dissociated in the presence of polyethylene glycol and mannitol. The circular dichroism spectra in the far UV indicated that the enzymes belong to the 13-13 family.


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