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Metabolic insights of lactic acid bacteria in reducing off-flavors and antinutrients in plant-based fermented dairy alternatives. [PDF]

Compr Rev Food Sci Food Saf
Molina GES, Ras G, da Silva DF, Duedahl-Olesen L, Hansen EB, Bang-Berthelsen CH.   +5 more
europepmc   +1 more source

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Glucosidases and galactosidases in soils

Soil Biology and Biochemistry, 1988
Abstract An improved method to assay activities of α- and β-glucosidases and α- and β-galactosidases in soils is described. It involves extraction and colorimetric determination of the p-nitrophenol released when 1 g of soil is incubated with 5 ml of buffered p-nitrophenyl glycoside solution at 37°C for 1 h.
F. Eivazi, M. Tabatabai
semanticscholar   +3 more sources

β-Glucosidases

Cellular and Molecular Life Sciences, 2010
β-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone
James R, Ketudat Cairns, Asim, Esen
openaire   +2 more sources

Glucosidases and exo-glucanases

Canadian Journal of Biochemistry, 1968
A comparison was made of exo-α-glucanases with α-glucosidases, and of exo-β1 → 3-glucanases with β-glucosidases to establish criteria for their characterization. Dimers, trimers, and tetramers of glucose are substrates for both exo-glucanases and glucosidases. Exo-glucanases act more rapidly on the longer oligomers, glucosidases on the shorter.
Frederick W. Parrish, Elwyn T. Reese, Anne Maguire   +2 more
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Immobilization of ?-D-Glucosidase and ?-D-Glucosidase-polyphenolic complexes

Biotechnology Letters, 1983
β-D-Glucosidase, alone and after copolymerizing with a resorcinol polymer, was immobilized on a PM 10 ultrafiltration membrane, κ-carrageenan and DEAE (DE52) cellulose. The best support for both enzyme preparations, in terms of high Vmax values, was the ultrafiltration membrane.
Sarkar, J M, Burns, Richard G
openaire   +3 more sources

Different inhibition properties of catechins on the individual subunits of mucosal α-glucosidases as measured by partially-purified rat intestinal extract.

Food & Function, 2019
Mucosal α-glucosidases from rat intestinal powder were employed, with a step to remove α-amylase, to measure the possibility of different inhibition of catechins, particularly those found in tea, on the four α-glucosidase enzymes. Inhibition of catechins
Jongbin Lim, Do Kyoung Kim, Hansol Shin, B. Hamaker, Byung-Hoo Lee   +4 more
semanticscholar   +1 more source

Yeast ß-Glucosidases

Biotechnology and Genetic Engineering Reviews, 1987
(1987). Yeast s-Glucosidases. Biotechnology and Genetic Engineering Reviews: Vol. 5, No. 1, pp. 269-296.
Alain Arnaud, R. Ratomahenina, Pierre Galzy, M. Leclerc   +3 more
openaire   +2 more sources

A simple kinetic test to distinguish exo-glucosidase and β-glucosidase activities

Biochemical and Biophysical Research Communications, 1985
Unusual kinetic behaviour was observed in assaying spectrophotometrically for exo-glucanase activity in a beta-glucosidase isolated from A. faecalis using p-nitrophenyl beta-cellobioside as substrate. At high substrate concentrations no phenol was released whereas at low concentrations a rapid release of phenol was detected and this increased in rate ...
Stephen G. Withers, Anthony G. Day
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Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides.

Journal of Agricultural and Food Chemistry, 2016
The mammalian mucosal α-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini).
Byung-Hoo Lee, D. Rose, A. Lin, R. Quezada‐Calvillo, B. Nichols, B. Hamaker   +5 more
semanticscholar   +1 more source