The performance of cellulase and amylase immobilized on siliceous supports was investigated. Enzyme uptake onto the support depended on the enzyme source and immobilization conditions. For amylase, the uptake ranged between 20 and 60%, and for cellulase, 7-10%. Immobilized amylase performance was assessed by batch kinetics in 100-300 g/L of corn flour at 65 degrees C. Depending on the substrate and enzyme loading, between 40 and 60% starch conversion was obtained. Immobilized amylase was more stable than soluble amylase. Enzyme samples were preincubated in a water bath at various temperatures, then tested for activity. At 105 degrees C, soluble amylase lost approximately 55% of its activity, compared with approximately 30% loss for immobilized amylase. The performance of immobilized cellulase was evaluated from batch kinetics in 10 g/L of substrate (shredded wastepaper) at 55 degrees C. Significant hydrolysis of the wastepaper was also observed, indicating that immobilization does not preclude access to and hydrolysis of insoluble cellulose.
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http://dx.doi.org/10.1385/abab:113:1-3:251 | DOI Listing |
Enzyme Microb Technol
December 2024
Guangxi Key Laboratory of Natural Polymer Chemistry and Physics, College of Chemistry and Materials, Nanning Normal University, Nanning 530001, PR China.
The immobilization of α-amylase and glucoamylase using a metal-organic framework (enzyme@ZIF-8) was prepared in situ through a one-pot method. The morphology, crystal structure, and molecular characteristics of the free enzyme and enzyme@ZIF-8 were characterized. The enzyme@ZIF-8 exhibited the rhombic dodecahedron morphology, with a decrease in particle size.
View Article and Find Full Text PDFIran J Microbiol
December 2024
Department of Biology, Faculty of Science, Farhangian University, Tehran, Iran.
Background And Objectives: The study focused on the amylase enzyme, widely used in the industrial starch liquefaction process. We looked into the best way to immobilize the native strain , which is the only alpha-amylase-producing bacterium, by trapping it in calcium alginate gel. This is a promising way to increase enzyme output.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Chemistry Department, Kurukshetra University, Kurukshetra 136119, Haryana, India. Electronic address:
The use of enzymes as catalysts in industrial processes has been studied, and they offer more ecologically friendly options for chemical reactions. In the current work, we investigated the potential of molecular modeling to solve the ordinarily difficult problem of identifying the amino acids involved in the covalent mode of immobilization by in silico investigations. The immobilized α-Amylase on Cellulose tosylate (henceforth referred to as Celltos) shows extra peaks of OH and NH, CN, SO, C-O-C, and CS.
View Article and Find Full Text PDFJ Adv Res
December 2024
Key Laboratory of Mesoscopic Chemistry (Ministry of Education), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, PR China. Electronic address:
Introduction: Weeds seriously affect crop yield in global agricultural production. Paraquat (PQ), as one of low cost and highly effective herbicide, is forbidden or severely restricted in production and sales owing to its lethal toxicity to humans. Creating an efficient and bio-friendly PQ formulation is crucial to facilitate the open use of PQ in world's agriculture.
View Article and Find Full Text PDFProtein Expr Purif
March 2025
Institute of Chemistry, Khwaja Fareed University of Engineering & Information Technology, 64200, Rahim Yar Khan, Pakistan. Electronic address:
α-amylases are vital biocatalysts that constitute a billion-dollar industry with a substantial and enduring global demand. Amylases hydrolyze the α-1,4-glycosidic linkages in starch polymers to generate maltose and malto-oligosaccharides subunits. Amylases are key enzymes that have promising applications in various industrial processes ranging from pharmaceutical, pulp and paper, textile food industries to bioremediation and biofuel sectors.
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