An organic solvent and surfactant stable α-amylase was obtained from soybean seeds. The direct and indirect effect of various organic solvents (non-polar, polar protic, and polar aprotic) and surfactants on the activity and stability of free enzyme was determined. The enzyme showed a very high catalytic efficiency and stabilization against most of the organic solvents and surfactants tested, ex...

Hybrid (1 -33 -4)-P-glucanases which contain an N-terminal region derived from the Bacillus amyloliquefaciens enzyme and a C-terminal region of the closely related B. macerans enzyme may exhibit a thermostability superior to both parental enzymes. A systematic series of hybrid enzymes were constructed in order to delineate the amino acid residues that affect protein stability. Hybrid enzymes wi...

Specifically designed co-solvent mixtures are an efficient way to enhance the kinetics of enzyme-catalyzed reactions without compromising enzyme stability; among them, several deep eutectic solvents have emerged as exciting for biocatalytic reactions. DESs nature allows one tailor enzyme-co-solvent interactions by using constituents diverse functional groups. In this work, influence co-solvents...

In this study, immobilization of partially purified almond (Amygdalus communis) β-galactosidase on Con A layered calcium alginate-cellulose beads was investigated. Immobilized β-galactosidase retained 72% of theinitial activity after crosslinking by glutaraldehyde. Both soluble and immobilized enzyme exhibited the samepH and temperature optima at pH 5.5 and 50ºC, respectively. Howev...

A thermostable β-glucosidase was effectively immobilized on alginate by the method of gel entrapment. After optimization of immobilized conditions, recovered enzyme activity was 60%. Optimum pH, temperature, kinetic parameters, thermal and pH stability, reusability, and storage stability were investigated. The K m and V max for immobilized β-glucosidase were estimated to be 5.0 mM and 0.64 U/ml...