Page last updated: 2024-08-24

glucose, (beta-d)-isomer and 2-nitrophenylgalactoside

glucose, (beta-d)-isomer has been researched along with 2-nitrophenylgalactoside in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hengstenberg, W; Schulte, D	1
Jorge, JA; Polizeli, Mde L; Terenzi, HF; Zanoelo, FF	1

Other Studies

2 other study(ies) available for glucose, (beta-d)-isomer and 2-nitrophenylgalactoside

Article	Year
Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis. Protein engineering, 2000, Volume: 13, Issue:7 Topics: Amino Acid Substitution; Amino Acids; Bacterial Proteins; beta-Galactosidase; Binding Sites; Escherichia coli; Galactosephosphates; Glucosides; Glycoside Hydrolases; Lactococcus lactis; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Structure, Tertiary; Recombinant Fusion Proteins; Species Specificity; Substrate Specificity	2000
Beta-glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose. FEMS microbiology letters, 2004, Nov-15, Volume: 240, Issue:2 Topics: Ascomycota; beta-Glucosidase; Cellobiose; Disaccharides; Enzyme Activators; Enzyme Induction; Enzyme Stability; Glucose; Glucosides; Glycosides; Hydrogen-Ion Concentration; Isoelectric Point; Lactose; Molecular Weight; Nitrophenylgalactosides; Substrate Specificity; Temperature; Xylose	2004

Article

Year

Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis.

Protein engineering, 2000, Volume: 13, Issue:7

Topics: Amino Acid Substitution; Amino Acids; Bacterial Proteins; beta-Galactosidase; Binding Sites; Escherichia coli; Galactosephosphates; Glucosides; Glycoside Hydrolases; Lactococcus lactis; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Structure, Tertiary; Recombinant Fusion Proteins; Species Specificity; Substrate Specificity

2000

Beta-glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose.

FEMS microbiology letters, 2004, Nov-15, Volume: 240, Issue:2

Topics: Ascomycota; beta-Glucosidase; Cellobiose; Disaccharides; Enzyme Activators; Enzyme Induction; Enzyme Stability; Glucose; Glucosides; Glycosides; Hydrogen-Ion Concentration; Isoelectric Point; Lactose; Molecular Weight; Nitrophenylgalactosides; Substrate Specificity; Temperature; Xylose

2004