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.
Protein & Peptide Letters
Title:Physicochemical properties and behavior in solution of three cellulases from haliotis fulgens
Volume: 7 Issue: 6
Author(s): Alejandra Hernandez-Santoyo, Arturo Rojo-Domfnguez, Enrique Garcfa-Hernandez and Adela Rodrfguez-Romero*
Affiliation:
- Instituto de Qufmica, Universidad Nacional Aut6noma de Mexico, Circuito Exterior, Ciudad llniversitaria, Coyoacan 04510. Mexico, D.F.
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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Cite this article as:
Hernandez-Santoyo Alejandra, Rojo-Domfnguez Arturo, Garcfa-Hernandez Enrique and Rodrfguez-Romero Adela*, Physicochemical properties and behavior in solution of three cellulases from haliotis fulgens, Protein & Peptide Letters 2000; 7 (6) . https://dx.doi.org/10.2174/092986650706221207163656
DOI https://dx.doi.org/10.2174/092986650706221207163656 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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