Results 81 to 90 of about 4,794 (208)
Retaining glycoside hydrolases are enzymes that catalyse the breakdown down of glycans through hydrolysis. Due to the double-replacement mechanism of the retaining glycoside hydrolases (GHs), which form an intermediate with part of the glycan covalently ...
Wiemann, Mathias,, Lund University.
core
Although enormous efforts have been made to prepare tasty and soluble steviol glycosides (SGs), the structure–property relationship of SGs still remains unclear, neither in experiment fact nor in the mechanism, such as the influence of linkage type and ...
Zhuoyu Zhou +4 more
doaj +1 more source
Human milk oligosaccharides (HMOs) signify a unique group of oligosaccharides in breast milk, which is of major importance for infant health and development.
Birgitte Zeuner +3 more
doaj +1 more source
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 +4 more
doaj +1 more source
Transglycosylation of Thiamin by Fungal β-N-Acetylhexosaminidases [PDF]
A new thiamin glycoside, e.g., thiamin β-D-2-deoxy-2-acetamidoglucopyranoside was prepared by transglycosylation by β-N-acetylhexosaminidase from Aspergillus oryzae and characterized spectrally. Series of other fungal β-N-acetyl-hexosaminidases from A. awamori, A. tamari, A. terreus, and Penicillium oxalicum were shown to be able to synthesize the same
KREN, Vladimir +3 more
openaire +2 more sources
The Formation of Covalent Linkages in Lignocellulosic Biomass via the Oxocarbenium Intermediate
Density functional theory models show that the hydrated and acidic hemicellulose matrix in lignocellulosic biomass can generate oxocarbenium ions. These reactive intermediates can participate in the stable formation of glycosidic lignin‐carbohydrate covalent linkages, promoting recalcitrance in plant biomass.
Eduardo Romero‐Montalvo +1 more
wiley +1 more source
Advancements in the Engineering Modification of Sucrose Phosphorylase
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 +3 more
doaj +1 more source
A structural perspective on α‐glucan catabolism in oxygenic phototrophs
SUMMARY Starch and glycogen are the main α‐glucan storage polymers in oxygenic photoautotrophs, ensuring metabolic continuity during day/night cycles and environmental stress. Their mobilization requires a suite of catabolic enzymes whose activities are tightly regulated to balance carbon storage with energy demands.
Sofia Doello, Dmitry Shvarev
wiley +1 more source
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 +4 more
doaj +1 more source
Al‐Hilfi et al. present a biocatalytic strategy for synthesizing 5‐methyl‐5,6‐dihydrothymidine (5‐MDHT), a sensitive MRI contrast agent. The study demonstrates that recombinant enzyme catalysis offers an efficient, sustainable, and eco‐friendly alternative to traditional chemical synthesis for producing clinically relevant imaging probes.
Aimen Al‐Hilfi +8 more
wiley +1 more source

