AmyUS100DELTAIG is designed to improve the thermostability of the thermoactive and thermostable maltohexaose forming alpha-amylase produced in Geobacillus stearothermophilus sp. US100, AmyUS100
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
coexpressed in a construct in Corynebacterium glutamicum, combined with Escherichia coli K-12 lysine decarboxylase for an one-step production of cadaverine, from soluble starch and the yield of cadaverine is 23.4 mM after 21 h. Construction of the Escherichia coli-Corynebacterium glutamicum shuttle vector, producing lysine decarboxylase under the control of the high constitutive expression promotor, and transformed this vector into Corynebaterium glutamicum. The engineered Corynebacterium glutamicum expresses both lysine decarboxlase and alpha-amylase, which retains their activity
improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C
improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C
design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm
design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm
starch has a protective effect on thermal stability of honey amylase. Therefore, it might be critical to process or control the amylase in honey before incorporation into starch-containing foods to aid in the preservation of starch functionality
the maltooligosaccharide forming endo-alpha-amylase is useful in bread making as an antistaling agent and it can be produced economically using low-cost sugarcane bagasse
the maltooligosaccharide forming endo-alpha-amylase is useful in bread making as an antistaling agent and it can be produced economically using low-cost sugarcane bagasse
the high cumulative activity and seven successive reuses obtained at liquefaction temperature render the covalently bound thermostable enzyme to calcium alginate matrix, a promising candidate for use in industrial starch hydrolysis process
the inhibition of alpha-amylase can significantly reduce the post-prandial increase of blood glucose and therefore can be an important strategy in the management of blood glucose level in type 2 diabetic and borderline patients
immobilization of enzyme in calcium alginate beads through entrapment technique. Activity of immobilized enzyme is 81% of free enzyme, its optimum acivity at pH 4.5-6.0 and 40°C, compared to pH 5.5 and 30°C for free enzyme. Immobilized enzyme retains its activity longer than free enzyme
use of probiotic Bacillus spores as a matrix for enzyme immobilization by covalent and adsorption methods. The maximum concentration of the alpha-amylase immobilized is 360 microg/1.2 10EE11spores. Maximum activity is achieved at an enzyme concentration of approximately 60 microg/0.4 10EE10 spores, corresponding to an estimated activity of 8000 IU per mg and 1.2 10EE11 spores for covalent immobilization and 85300 IU for the adsorption method. Enzyme immobilization yield is estimated to be 77% and 20.07% for the covalent and adsorption methods, respectively. The alpha-amylase immobilized by both methods, displays improved activity in the basic pH range. The optimum pH for the free enzyme is 5 while it shifts to 8 for the immobilized enzyme. The optimum temperatures for the free and immobilized enzymes are 0C and 0C, respectively. The covalently immobilized alpha-amylase retains 65% of its initial activity, even after 10 times of recycling
cold-active alpha-amylase from mutant Microbacterium foliorum strain GA2 can be profitably used in detergents for laundry and automatic dishwashing to degrade the residues of starchy foods
cold-active alpha-amylase from mutant Microbacterium foliorum strain GA2 can be profitably used in detergents for laundry and automatic dishwashing to degrade the residues of starchy foods