Cellulosic exopolysaccharide produced by Zoogloea sp. as a film support for trypsin immobilisation |
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| Institution: | 1. Departamento de Química, Universidade Estadual de Londrina, Campus Universitário, Rod. Celso Garcia Cid, PR 445 Km 380, Londrina, PR, CEP 86051-990, Brazil;2. Centro de Ciências Agrárias, Universidade Estadual do Oeste do Paraná, Rua Pernambuco, n. 1777, Marechal Cândido Rondon, PR, CEP 85960-000, Brazil;3. Instituto Nacional de Ciência e Tecnologia (INCT) de Bioanalítica, Universidade Estadual de Campinas (UNICAMP), Instituto de Química, Departamento de Química Analítica, Cidade Universitária Zeferino Vaz s/n, Campinas, SP, CEP 13083-970, Brazil;1. Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng 252059, PR China;2. Shandong Provincial Key Laboratory of Chemical Energy Storage and Novel Cell Technology, Liaocheng University, Liaocheng 252059, PR China;3. Institute of Immunology and Molecular Medicine, Jining Medical University, Jining 272067, PR China;1. School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou 450001, PR China;2. Vocational College of Water Conservancy and Environment, Zhengzhou 450001, PR China;3. School of International Education, Henan University of Technology, Zhengzhou 450001, PR China;4. College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, PR China |
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| Abstract: | Trypsin (E.C. 3.4.21.4) was covalently immobilised onto a membrane of a cellulosic exopolysaccharide produced by Zoogloea sp. in sugarcane molasses. Carbonyl groups were introduced into the matrix by sodium metaperiodate oxidation and the enzyme was immobilised either directly or through bovine serum albumin (BSA) as a spacer. The trypsin-membrane and trypsin–BSA-membrane retained, respectively, 37.2% and 9.16% of the specific activity of the native enzyme acting on N-benzoil-dl-arginine-p-nitroanilide (BAPNA). No activity decrease was observed in both preparations after seven reutilisations as well as they showed to be more thermal stable than the native enzyme. The trypsin–BSA-membrane presented the same initial activity (99%) after 54 days stored in 0.1 M Tris–HCl buffer, pH 8.0, at 4 °C but the trypsin-membrane lost 15% of activity. Furthermore, the trypsin–BSA-membrane lost 31% of activity after reuse at 9 days interval during 54 days of storage at 4 °C whereas the trypsin-membrane lost 69% of activity under the same conditions. These results showed an additional application for this biofilm, namely, to act as a reusable matrix for trypsin immobilisation and the presence of BSA improved the derivative performance. |
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