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- Hwa, Kuo Yuan; Subramani, Boopathi; Shen, San-Tai; Lee, Yu-May
- Enzyme and microbial technology 2015 v.77 pp. 14-20
- Lewis bases; Thermococcus kodakarensis; active sites; beta-galactosidase; beta-glucosidase; beta-mannosidase; catalytic activity; cellulose; enzyme activity; hyperthermophilic archaea; moieties; mutants; polyacrylamide gel electrophoresis; sequence alignment; substrate specificity; temperature; thermal stability; thermostable enzymes
- ... β-Glycosidase from Thermococcus kodakarensis KOD1 is a hyperthermophilic enzyme with β-glucosidase, β-mannosidase, β-fucosidase and β-galactosidase activities. Sequence alignment with other β-glycosidases from hyperthermophilic archaea showed two unique active site residues, Gln77 and Asp206. These residues were represented by Arg and Asp in all other hyperthermophilic β-glycosidases. The two acti ...
- Santos, Jose C.S. dos; Rueda, Nazzoly; Gonçalves, Luciana R.B.; Fernandez-Lafuente, Roberto
- Enzyme and microbial technology 2015 v.77 pp. 1-7
- Lewis bases; Pseudozyma antarctica; Thermomyces lanuginosus; agarose; biocatalysts; butyrates; carboxylic ester hydrolases; enzyme activity; enzyme stability; pH; phenylacetic acid; solvents; thermal stability
- ... Lipase from Thermomyces lanuginosus (TLL) and lipase B from Candida antarctica (CALB) have been immobilized on divinylsulfone (DVS) activated agarose beads at pH 10 for 72h. Then, as a reaction end point, very different nucleophiles have been used to block the support and the effect of the nature of the blocking reagent has been analyzed on the features of the immobilized preparations. The blockin ...