Results 131 to 140 of about 5,631 (193)

Safety evaluation of an extension of use of the food enzyme β-galactosidase from the genetically modified <i>Bacillus licheniformis</i> strain NZYM-BT. [PDF]

EFSA J
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Cavanna D, Liu Y, Tokić V.   +15 more
europepmc   +1 more source

Effect of Galacto-oligosaccharides with Different Degrees of Polymerization on the Storage Stability of Freeze-Dried Lecithin Liposomes. [PDF]

Foods
Faroux JM, Ureta M, Gomez-Zavaglia A, Tymczszyn EE.   +3 more
europepmc   +1 more source

Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion. [PDF]

Nat Microbiol
Bakshani CR, Ojuri TO, Pilgaard B, Holck J, McInnes R, Kozak RP, Zakhour M, Çakaj S, Kerouedan M, Newton E, Bolam DN, Crouch LI.   +11 more
europepmc   +1 more source

Recombinant Production and Characterization of Six Novel GH27 and GH36 α-Galactosidases From Penicillium Subrubescens and Their Synergism With a Commercial Mannanase During the Hydrolysis of Lignocellulosic Biomass [PDF]

Bioresource Technology, 2020
α-Galactosidases are important industrial enzymes for hemicellulosic biomass degradation or modification. In this study, six novel extracellular α-galactosidases from Penicillium subrubescens were produced in Pichia pastoris and characterized.
Henrik Stålbrand, Ronald P de Vries, Adiphol Dilokpimol   +2 more
exaly   +4 more sources

Spectroscopic and Thermodynamic Properties of Debaryomyces hansenii UFV-1 α-Galactosidases

International Journal of Biological Macromolecules, 2010
Spectroscopic and thermodynamic properties were determined for Debaryomyces hansenii UFV-1 extracellular and intracellular α-galactosidases. α-Galactosidases showed similar secondary structure compositions (α-helix, β-sheet parallel and β-turn).
Ronaldo A P Nagem, Alexandre Santos, Marcelo M Santoro   +2 more
exaly   +2 more sources

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β-Galactosidase

Cold Spring Harbor Protocols, 2017
β-galactosidase is used as a reporter for the quantitative analysis of gene expression. It is also used as a histochemical marker. This introduction briefly reviews the enzymatic reactions catalyzed by β-galactosidase and methods for assaying β-galactosidase activity.
Pradeep D, Uchil, Arvindhan, Nagarajan, Priti, Kumar   +2 more
openaire   +2 more sources

The discovery of β-galactosidase

Trends in Biochemical Sciences, 1989
The enzyme beta-galactosidase was first mentioned in the literature by Beijerinck exactly a hundred years ago. The Department of Microbiology and Enzymology of the Delft University of Technology keeps the memory of Beijerinck, its first professor, alive by maintaining a 'Beijerinck-room' in the attic of the building.
Rouwenhorst, R.J. (author), Pronk, J.T. (author), Van Dijken, J.P. (author)   +2 more
openaire   +3 more sources

Plasma α-galactosidase A: Properties and comparisons with tissue α-galactosidases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
The human plasma form of alpha-galactosidase A (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) was highly purified and exhibited apparent Km values of 1.9 mM with 4-methylumbelliferyl-alpha-D-galactopyranoside and 0.23 mM with globotriglycosylceramide.
D F, Bishop, C C, Sweeley
openaire   +2 more sources

Association Between the Organoleptic Scores, Oral Condition and Salivary β-Galactosidases in Children Affected by Halitosis

International Journal of Dental Hygiene, 2014
Objectives: The goal of this work is to evaluate the association between organoleptic scores, oral condition and salivary b-galactosidases, to facilitate the differential diagnosis of halitosis in children.
Morena Petrini, Giuseppe Spoto, R Docimo
exaly   +2 more sources

The assay of β-galactosidase in soil

Folia Microbiologica, 1972
The method for the assay of β-galactosidase introduced by Lederberg (1950) was modified and used for studies of the enzyme in the soil.o-Nitrophenyl-β-d-galactoside served as substrate. Trismaleinate buffer was found to be more suitable than phosphate buffer in the assay.
P, Rysavý, J, Macura
openaire   +2 more sources