Journal of Chemical Technology & Biotechnology · 1990 · 55 citations · 17 references
Life SciencesBiochemistryBiotechnologyBiocatalysisBiochemical EngineeringEnzymologyEnzyme CharacterizationEnzyme ImmobilizationEnzyme KineticsEnzyme-substrate RecognitionFood EnzymesImmobilized EnzymesCarbohydrate Hydrolysis By Alpha-amylaseDiffusion ResistanceDiffusional EffectsEnzyme Immobilization On Solid SupportsPorous SilicaPorous Silica MaterialsSilica SupportsTransglycosylation
Alpha-amylase from Aspergillus oryzae has been immobilized onto corn grits and porous silica (specific areas 180 and 440 m2 g-1). Kinetic parameters of immobilized enzyme have been determined. Immobilization of alpha-amylase results in the formation of less polymerized products resulting in an apparent decrease in the number of transglycosylation reactions, for both maltotetraose and starch as substrates, when compared with free enzyme. Diffusional limitations for substrate and products have been quantified in the case of the three supports used. External diffusional resistances were important in all cases for the reaction products, whilst they became negligible for the substrate in the case of silica supports. Moreover, internal transfer limitations were identified with silica 180 m2 g-1 support. It was demonstrated that diffusional resistances were in direct relation to the apparent modification of the enzyme action pattern after immobilization.
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The properties of gases and liquids
Choice Reviews Online · 2001 · 13K citations
Natural Sciences, Chemistry, Physics +10
Structure and Possible Catalytic Residues of Taka-Amylase A
Y. Matsuura, Masami Kusunoki, Wakako Harada et al. · The Journal of Biochemistry · 1984 · 643 citations
Microbial enzymes and biotechnology
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