Results 41 to 50 of about 1,138 (192)

Recombinant microbial systems for improved β-galactosidase production and biotechnological applications [PDF]

open access: yes, 2011
β-Galactosidases (EC 3.2.1.23) constitute a large family of proteins that are known to catalyze both hydrolytic and transgalactosylation reactions. The hydrolytic activity has been applied in the food industry for decades for reducing the lactose content
Domingues, Lucília   +2 more
core   +1 more source

Characterization of β-galactosidase and α-galactosidase activities from the halophilic bacterium Gracilibacillus dipsosauri

open access: yesAnnals of Microbiology, 2021
Purpose Gracilibacillus dipsosauri strain DD1 is a salt-tolerant Gram-positive bacterium that can hydrolyze the synthetic substrates o-nitrophenyl-β-d-galactopyranoside (β-ONP-galactose) and p-nitrophenyl-α-d-galactopyranoside (α-PNP-galactose).
Charles E. Deutch   +2 more
doaj   +1 more source

Biocatalytic approaches using lactulose: end product compared with substrate [PDF]

open access: yes, 2016
Lactulose is a lactose-based carbohydrate with well-known prebiotic effect and recognized medical applications. Currently, the commercially available lactulose is chemically synthesized. Nevertheless, the process leads to low yields and high levels of by-
Macedo, Eugénia A.   +3 more
core   +2 more sources

Biochemical characterization of three Aspergillus niger β-galactosidases

open access: yesElectronic Journal of Biotechnology, 2017
Background: β-Galactosidases catalyze both hydrolytic and transgalactosylation reactions and therefore have many applications in food, medical, and biotechnological fields.
Dandan Niu   +7 more
doaj   +1 more source

Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS) [PDF]

open access: yes, 2017
The β-galactosidase from Bacillus circulans was covalently attached to aldehyde-activated (glyoxal) agarose beads and assayed for the continuous production of galactooligosaccharides (GOS) in a packed-bed reactor (PBR).
Ballesteros Olmo, Antonio   +4 more
core   +1 more source

Galactooligosaccharides production by β-galactosidase immobilized onto magnetic polysiloxane–polyaniline particles [PDF]

open access: yes, 2009
Magnetized polysiloxane coated with polyaniline (mPOS–PANI) was used as a support for β-galactosidase immobilization via glutaraldehyde. The galactooligosaccharides (GOS) production by this derivative was investigated under different initial lactose ...
Balcão, V. M.   +5 more
core   +1 more source

UV spectrophotometry method for the monitoring of galacto-oligosaccharides production [PDF]

open access: yes, 2009
Monitoring the industrial production of galacto-oligosaccharides (GOS) requires a fast and accurate methodology able to quantify, in real time, the substrate level and the product yield.
Correia, Daniela M.   +7 more
core   +3 more sources

Galactooligosaccharides: production, health benefits, application to foods and perspectives

open access: yesScientia Agropecuaria, 2015
Synthesized from lactose transgalactosylation, galactooligosaccharides are non-digestible carbohydrates classified as prebiotic ingredients of high added value.
Ana Elizabeth Cavalcante Fai   +1 more
doaj   +1 more source

Galacto-oligosaccharides production during lactose hydrolysis by free Aspergillus oryzae β-galactosidase and immobilized on magnetic polysiloxane-polyvinyl alcohol [PDF]

open access: yes, 2009
The synthesis of galacto-oligosaccharides (GOS) by the action of Aspergillus oryzae β-galactosidase free and immobilized on magnetic polysiloxane-polyvinyl alcohol (mPOS-PVA) was studied.
Balcão, V. M.   +8 more
core   +1 more source

Transgalactosylation activity of ebg beta-galactosidase synthesizes allolactose from lactose [PDF]

open access: yesJournal of Bacteriology, 1982
ebg enzyme, the second beta-galactosidase of Escherichia coli, does not normally convert lactose into an inducer of the lac operon. We previously reported the existence of a mutant ebg enzyme that does make such an inducer in vivo (Rolseth et al., J. Bacteriol. 142:1036-1039, 1980).
openaire   +2 more sources

Home - About - Disclaimer - Privacy