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Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles
Carneiro, Lara Aparecida Buffoni Campos; Costa-Silva, Tales Alexandre; Souza, Cláudia Regina Fernandes; Bachmann, Luciano; Oliveira, Wanderley Pereira; Said, Suraia.
  • Carneiro, Lara Aparecida Buffoni Campos; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
  • Costa-Silva, Tales Alexandre; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
  • Souza, Cláudia Regina Fernandes; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
  • Bachmann, Luciano; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
  • Oliveira, Wanderley Pereira; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
  • Said, Suraia; Universidade de São Paulo. Faculdade de Ciências Farmacêuticas de Ribeirão Preto. Departamento de Ciências Farmacêuticas. Ribeirão Preto. BR
Braz. arch. biol. technol ; 57(4): 578-586, Jul-Aug/2014. tab, graf
Article in English | LILACS-Express | LILACS | ID: lil-712932
Responsible library: BR1.1
ABSTRACT
This work studied the immobilization of Cercospora kikuchii lipases on chitosan microparticles by chemical attachment on chitosan acetate microparticles activated by glutaraldehyde (CAM) added before or after the enzyme and physical adsorption on highly deacetylated chitosan hydrochloride microparticles (CHM). Lipases covalently immobilized on pre-activated CAM showed better performance retaining 88.4% of the enzymatic activity, with 68.2% of immobilization efficiency (IE). The immobilized enzyme retained an activity of about 53.5 % after five reuses, using p-NPP as substrate. Physical adsorption of lipase onto highly deacetylated CHM showed 46.2 % of enzymatic activity and 28.6% of IE. This immobilized derivative did not lose activity up to 80 days of storage at 4°C, while lipases immobilized on pre-activated CAM maintained its activity up to 180 days at same conditions. Taken together the results indicate that chitosan microparticles provide an optimal microenvironment for the immobilized enzyme to maintain good activity and stability.


Full text: Available Index: LILACS (Americas) Language: English Journal: Braz. arch. biol. technol Journal subject: Biology Year: 2014 Type: Article / Project document Affiliation country: Brazil Institution/Affiliation country: Universidade de São Paulo/BR

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Full text: Available Index: LILACS (Americas) Language: English Journal: Braz. arch. biol. technol Journal subject: Biology Year: 2014 Type: Article / Project document Affiliation country: Brazil Institution/Affiliation country: Universidade de São Paulo/BR