Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant-Reference-Cited by-同舟云学术

Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant

Published:2013-06 Issue: Volume:75 Page:32-38
ISSN:1369-703X
Container-title:Biochemical Engineering Journal
language:en
Short-container-title:Biochemical Engineering Journal

Author:

Escobar Sindy,Bernal Claudia,Mesa Monica

Publisher

Elsevier BV

Subject

Biomedical Engineering,Environmental Engineering,Bioengineering,Biotechnology

Reference48 articles.

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2. Separation and characterization of three β-galactosidases from Bacillus circulans;Vetere;Biochim. Biophys. Acta,1998

3. Galacto-oligosaccharide synthesis from lactose solution or skim milk using the β-galactosidase from Bacillus circulans;Rodriguez-Colinas;J. Agric. Food Chem.,2012

4. Kinetics and design relation for enzymatic conversion of lactose into galacto-oligosaccharides using commercial grade β-galactosidase;Palai;J. Biosci. Bioeng.,2012

5. J. Nelms, I. G. Fotheringham, Two new -d-galactosidases from Bacillus circulans: a common sequence homology surrounding the putative active site region in several -glycosidase families, Uniprot database (entry Q45093 encodes a protein of 690 AA; entry O31341 encodes a protein of 586 AA).

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