Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor
Autor: | F. F. Freitas, Taciana Soares do Carmo, Larissa Nayhara Soares Santana Falleiros, Bruna Vieira Cabral, Saulo Luiz Cardoso, Miriam Maria de Resende, Eloízio Júlio Ribeiro, Líbia Diniz Santos |
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Rok vydání: | 2017 |
Předmět: |
0106 biological sciences
Packed bed Chromatography Immobilized enzyme Central composite design 010405 organic chemistry General Chemical Engineering Batch reactor General Chemistry equipment and supplies 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Hydrolysis Adsorption Invertase chemistry 010608 biotechnology Glutaraldehyde |
Zdroj: | Chemical Engineering Communications. 204:1007-1019 |
ISSN: | 1563-5201 0098-6445 |
Popis: | The conversion of sucrose to a highly concentrated commercial syrup by immobilized invertase by combining the processes of adsorption and cross-linking using Duolite A-568 as the carrier was studied. Central Composite Design (CCD) was used to assess the effect of glutaraldehyde concentration and cross-linking reaction time on immobilized enzyme activity throughout the hydrolysis of sucrose in a batch reactor. Cross-linking optimization allowed us to find the optimum conditions for activity with a glutaraldehyde concentration of 0.6 g · L−1 and a cross-linking time of 6 h. The temperature and pH that maximized the activity of the immobilized biocatalyst in the cross-linking process were 50°C and 4.0, respectively. Cross-linking allows the biocatalyst to be active at higher temperatures and lower pH. High-sucrose conversions to invert sugar using a continuous fixed-bed reactor were obtained. The immobilized biocatalyst also demonstrated greater thermal stability at low temperatures. |
Databáze: | OpenAIRE |
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