Maltotriosyl-erythritol, a transglycosylation product of erythritol by Thermus sp. amylomaltase and its application to prebiotic.

In this study, maltotriosyl-erythritol (EG) was synthesized as a novel prebiotic candidate via transglycosylation using recombinant amylomaltase (AMase) from Thermus sp. Tapioca starch served as the glucosyl donor, and erythritol as the acceptor. High-performance liquid chromatography (HPLC) revealed an EG yield of 14.

Enzymatic Synthesis of Maltitol and Its Inhibitory Effect on the Growth of DMST 18777.

This study aimed to synthesize maltitol using recombinant CGTase from A11 with β-cyclodextrin (β-CD) and sorbitol as a glucosyl donor and acceptor, respectively, and assess its antibacterial activity. Optimal conditions for producing the highest yield, 25.0% (/), were incubation of 1% (/) β-CD and sorbitol with 400 U/mL of CGTase in 20 mM phosphate buffer at pH 6.

Optimization of amylomaltase for the synthesis of α-arbutin derivatives as tyrosinase inhibitors.

α-Arbutin is widely used as a skin-whitening agent in the pharmaceutical and cosmetic industries because of its inhibitory effect on tyrosinase, an important enzyme for generating melanin pigments. Given the increasing demand for such products, we synthesized α- and β-arbutin-α-D-glycosides through transglycosylation reactions catalyzed by a recombinant amylomaltase, using tapioca starch and α- and β-arbutin as donor and acceptor molecules, respectively. The catalytic yield of products by the amylomaltase was greater with α-arbutin than with β-arbutin.

Application of amylomaltase for the synthesis of salicin-α-glucosides as efficient anticoagulant and anti-inflammatory agents.

The focus of this study was the synthesis of α-glucosyl derivatives of salicin by a transglucosylation reaction. The reaction was catalyzed by recombinant amylomaltase using tapioca starch as a glucosyl donor. Several reaction parameters, such as the enzyme-substrate concentrations, pH, temperature and incubation time, were optimized.

Kinetic inhibition of human salivary alpha-amylase by a novel cellobiose-containing tetrasaccharide.

Objective: The aim of the study was to evaluate the inhibitory kinetics of a novel cellobiose-containing tetrasaccharide on human salivary alpha-amylase (HSA).

Material And Method: Synthesis of cellobiose-containing tetrasaccharide was catalyzed by Paenibacillus sp. All CGTase using beta-CD as a donor and cellobiose as an acceptor under the optimal conditions.

Effect of temperature on cyclodextrin production and characterization of paracetamol/cyclodextrin complexes.

Objective: To compare the effect of different reaction temperatures on the cyclization and coupling reactions of the Toruzyme CGTase influencing the yield of cyclodextrins (CDs) and to study the solubility of paracetamol with CDs.

Material And Method: Type and amount of CDs were analyzed by HPAEC-PAD. The stability constants for the inclusion complex formed between CDs and paracetamol were determined using the phase solubility method.