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Immobilized enzyme
About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.
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TL;DR: The laccase-glutaraldehyde-CF achieved excellent results in the clarification of apple juice, reducing 61 ± 1% of the original juice color and 29 ±- 1% of its turbidity, retaining up to 100% ofThe initial activity after a 10-times reuse assay.
90 citations
TL;DR: The influence of polyhydric alcohols and carbohydrates on the thermostability of Bacillus licheniformis α‐amylase was studied in the temperature range 96° to 130°C to show biphasic then first‐order inactivation kinetics, depending on the additive concentration and temperature.
Abstract: The influence of polyhydric alcohols and carbohydrates on the thermostability, i.e., the heat inactivation kinetics, of Bacillus licheniformis α-amylase was studied in the temperature range 96° to 130°C. High concentrations (from 9 to 60 weight percent) of glycerol, sorbitol, mannitol, sucrose, or starch can markedly decrease the inactivation rate constant, k, and in the studied cases, this stabilizing effect grows stronger with increasing additive concentration. Statements about stabilization should, however, be specified carefully with respect to temperature, because EA is mostly altered likewise. For dissolved enzyme EA was almost always decreased in the presence of polyol or carbohydrate, whereas for immobilized enzyme it was augmented in each studied instance. The inactivation of dissolved enzyme can, in all the studied cases, be adequately described as a firstorder process. Immobilized enzyme, however, shows biphasic then first-order inactivation kinetics, depending on the additive concentration and temperature. © 1994 John Wiley & Sons, Inc.
90 citations
TL;DR: The optimized parameters for the measurement procedure were determined and the detection limits were found to be 10 −12 M for DFP and 10 −6 M for paraoxon-methyl and trichlorfon.
90 citations
TL;DR: Firefly luciferase was entrapped in sol-gel-derived silica containing precursors based on covalent linkage of d-gluconolactone or d-maltonolact one to form N-(3-triethoxysilylpropyl)glu Conamide or N-( 3-triETHoxysilane)maltonamide and showed catalytic constants close to those in solution.
Abstract: Firefly luciferase (FL) was entrapped in sol−gel-derived silica containing precursors based on covalent linkage of d-gluconolactone or d-maltonolactone to (aminopropyl)triethoxysilane to form N-(3-triethoxysilylpropyl)gluconamide or N-(3-triethoxysilylpropyl)maltonamide. The enzyme was active and stable in this material and showed catalytic constants close to those in solution. As little as 20 amol ATP could be detected with the entrapped FL, and the entrapped enzyme could be used over several cycles.
90 citations
TL;DR: Neutrase, a commercial preparation of Bacillus subtilis, was covalently immobilized on alginate-glutaraldehyde beads and exhibited higher K(m) compared to the soluble enzyme, and the pH-activity profile was widened upon immobilization.
Abstract: Neutrase, a commercial preparation of Bacillus subtilis, was covalently immobilized on alginate−glutaraldehyde beads. Immobilization conditions and characterization of the immobilized enzyme were investigated. Central composite design and response surface methods were employed to evaluate the effects of immobilization parameters, such as glutaraldehyde concentration, enzyme loading, immobilization pH, and immobilization time. Under optimized working conditions (2% alginate, 6.2% glutaraldehyde, 61.84 U mL−1 Neutrase, pH 6.2, and 60 min) the immobilization yield was about 50%. The immobilized enzyme exhibited higher Km compared to the soluble enzyme. The pH−activity profile was widened upon immobilization. The optimum temperature was shifted from 50 to 60 °C, and the apparent activation energy was decreased from 47.7 to 22.0 kJ mol−1 by immobilization. The immobilized enzyme also showed significantly enhanced thermal stability.
90 citations