EC Number   |
Application |
Reference |
|---|
    3.2.1.1 | agriculture |
possilbe target in mite control |
707289 |
| 3.2.1.1 | analysis |
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 |
679943 |
| 3.2.1.1 | analysis |
the alpha-amylase from Anoxybacillus amylolyticus could be used in a sensitive method to detect very low concentrations of heavy metals |
-, 695097 |
| 3.2.1.1 | biofuel production |
the recombinant enzyme can be utilized for bioethanol production from jackfruit seed starch |
-, 750980 |
| 3.2.1.1 | biotechnology |
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 |
690597 |
| 3.2.1.1 | biotechnology |
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 |
-, 729490 |
| 3.2.1.1 | biotechnology |
the thermotolerant, glucose tolerant maltooligosaccharide-forming alpha-amylase is potent for biotechnological application |
-, 678799 |
| 3.2.1.1 | brewing |
important industrial enzyme in brewing and alcohol production |
726490 |
| 3.2.1.1 | detergent |
AmyUS100DELTAIG is designed to improve the thermostability of the thermoactive and thermostable maltohexaose forming alpha-amylase produced in Geobacillus stearothermophilus sp. US100, AmyUS100 |
691421 |
| 3.2.1.1 | energy production |
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 |
-, 748768 |
