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Título

Enzymatic generation of chitooligosaccharides from chitosan using soluble and immobilized glycosyltransferase (Branchzyme)

AutorMontilla, Antonia ; Ruiz-Matute, Ana I. ; Corzo, Nieves ; Giacomini, Cecilia; Irazoqui, Gabriela
Palabras claveImmobilization
Branchzyme
COS
Chitooligosaccharides
HPLC−SEC
GC−FID
MALDI-TOF
Fecha de publicación2013
EditorAmerican Chemical Society
CitaciónJournal of Agricultural and Food Chemistry 61(43): 10360-10367 (2013)
ResumenChitooligosaccharides possessing remarkable biological properties can be obtained by enzymatic hydrolysis of chitin. In this work, the chitosanase activity of soluble and immobilized glycosyltransferase (Branchzyme) toward chitosan and biochemical characterization are described for the first time. This enzyme was found to be homotetrameric with a molecular weight of 256 kDa, an isoelectric point of 5.3, and an optimal temperature range of between 50 and 60 °C. It was covalently immobilized to glutaraldehyde–agarose with protein and activity immobilization yields of 67% and 17%, respectively. Immobilization improved enzyme stability, increasing its half-life 5-fold, and allowed enzyme reuse for at least 25 consecutive cycles. The chitosanase activity of Branchzyme on chitosan was similar for the soluble and immobilized forms. The reaction mixture was constituted by chitooligosaccharides with degrees of polymerization of between 2 and 20, with a higher concentration having degrees of polymerization of 3–8.
Versión del editorhttps://doi.org/10.1021/jf403321r
URIhttp://hdl.handle.net/10261/99979
DOI10.1021/jf403321r
Identificadoresdoi: 10.1021/jf403321r
issn: 0021-8561
e-issn: 1520-5118
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