Results 81 to 90 of about 5,064 (210)

Transglycosylating β‐d‐galactosidase and α‐l‐fucosidase from Paenibacillus sp. 3179 from a hot spring in East Greenland

MicrobiologyOpen, 2020
Thermal springs are excellent locations for discovery of thermostable microorganisms and enzymes. In this study, we identify a novel thermotolerant bacterial strain related to Paenibacillus dendritiformis, denoted Paenibacillus sp.
Mariane S. Thøgersen, Stefan J. Christensen, Morten Jepsen, Lars H. Pedersen, Peter Stougaard   +4 more
doaj   +1 more source

Improved Transglycosylation by a Xyloglucan-Active α-l-Fucosidase from Fusarium graminearum

Journal of Fungi, 2020
Fusarium graminearum produces an α-l-fucosidase, FgFCO1, which so far appears to be the only known fungal GH29 α-l-fucosidase that catalyzes the release of fucose from fucosylated xyloglucan.
Birgitte Zeuner, Marlene Vuillemin, Jesper Holck, Jan Muschiol, Anne S. Meyer   +4 more
doaj   +1 more source

Exploring Diverse Glycone Preferences of Aspergillus rutinosidases

Advanced Synthesis &Catalysis, Volume 368, Issue 11, 3 June 2026.
Rutinosidases from Aspergillus niger (AnRut) and A. oryzae (AoRut) catalyze hydrolysis and transglycosylation with non‐natural glycosides as donors, enabling glycosylation of alcoholic and phenolic acceptors. AnRut exhibits broad glycone promiscuity, while AoRut has a narrower substrate scope.
Jitka Brouzdová, Lucie Petrásková, Katerina Brodsky, Natalia Kulik, Helena Pelantová, Martina Hurtová, Andrea Vopálenská, Kristýna Slámová, Pavla Bojarová, Vladimír Křen   +9 more
wiley   +1 more source

Contribution of W229 to the transglycosylation activity of 4-α-glucanotransferase from Pyrococcus furiosus

, 2006
A W229H mutant of 4-α-glucanotransferase (4-α-GTase) from Pyrococcus furiosus was constructed and its catalytic properties were studied to investigate the role of W229 in the catalytic specificities of the enzyme.
H Cha, K H Park, Eui-Jeon Woo, S Y Tang, S J Yang, C Park   +5 more
core   +1 more source

Advancements in the Engineering Modification of Sucrose Phosphorylase

Crystals
Sucrose phosphorylase (SPase) is a member of the glycoside hydrolase family 13, catalyzing the reversible phosphorolysis of sucrose to produce α–glucose–1–phosphate and exhibiting transglycosylation activity toward multiple substrates. Its wide substrate
Shuru Ma, Hongyu Zhang, Tingting Lou, Suying Wang   +3 more
doaj   +1 more source

Comprehensive and Comparative Transcriptional Profiling of the Cell Wall Stress Response in Bacillus subtilis

Molecular Microbiology, Volume 125, Issue 6, Page 506-545, June 2026.
Transcriptional profiling of the primary cell envelope stress response (CESR) of Bacillus subtilis exposed to a range of cell wall‐targeting antimicrobials, combining RNAseq and high‐resolution tiling arrays. We revealed the complexity of the CESR, the contribution of extracytoplasmic function sigma factors (ECFs) and two‐component signal transduction ...
Qian Zhang, Charlène Cornilleau, Lena Friebel, Sarah Spitzner, Raphael R. Müller, Doreen Meier, Pierre Flores, Cyprien Guérin, Pierre Nicolas, Diana Wolf, Vincent Fromion, Rut Carballido‐López, Thorsten Mascher   +12 more
wiley   +1 more source

Transglycosylation Action of Amylases

Journal of the Japanese Society of Starch Science, 1973
By using the substrates of defined anomeric form, with very brief incubation to limit mutarotation, evidence has been obtained that the condensations require donor substrates of specific configuration. That is, crystalline glucoamylase from Rh, niveus has been found to catalyze the rapid synthesis of maltose and a slower synthesis of isomaltose ...
openaire   +2 more sources

Safety evaluation of an extension of use of the food enzyme β‐galactosidase from the genetically modified Bacillus licheniformis strain NZYM‐BT

EFSA Journal, Volume 24, Issue 6, June 2026.
Abstract The food enzyme β‐galactosidase (EC 3.2.1.23) is produced with the genetically modified Bacillus licheniformis strain NZYM‐BT by Novozymes A/S. The safety of this food enzyme was evaluated previously, and no safety concern was identified when used in one food manufacturing process.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Daniele Cavanna, Yi Liu, Valentina Tokić   +15 more
wiley   +1 more source

Beta-galactosidase activity in psychrotrophic microorganisms and their potential use in food industry

Czech Journal of Food Sciences, 2002
Twenty-one psychrotrophic resp. psychrophilic bacterial strains were screened for presence of b-galactosidase activity which showed 8 of them. b-Galactosidase activity of these strains was determined for 2 substrates - synthetic substrate (ONPG) and ...
P. Karasová, V. Spiwok, Š. Malá, B. Králová, N.J. Russell   +4 more
doaj   +1 more source

A Single Hydrogen Bond Controls the Selectivity of Transglycosylation vs Hydrolysis in Family 13 Glycoside Hydrolases

Converting glycoside hydrolases (GHs) from hydrolytic to synthetic enzymes via transglycosylation is a long-standing goal for the biosynthesis of complex carbohydrates.
Lingqia Su (3150570), Wei Xia (349131), Lei Wang (6656), Sheng Chen (21971), Binju Wang (1419697), Carme Rovira (1275285), Jing Wu (54032), Zhiyong Guo (110695), Isabelle André (1478674)   +8 more
core   +2 more sources