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Algal polysaccharides as matrices for the immobilization of urease in lipid ultrathin films studied with tensiometry and vibrational spectroscopy: Physical-chemical properties and implications in the enzyme activity.
de Brito, Audrey Kalinouski; Nordi, Cristina S F; Caseli, Luciano.
Afiliação
  • de Brito AK; Instituto de Ciências Ambientais, Químicas e Farmacêuticas, Universidade Federal de São Paulo, UNIFESP, Diadema, SP, Brazil.
  • Nordi CSF; Instituto de Ciências Ambientais, Químicas e Farmacêuticas, Universidade Federal de São Paulo, UNIFESP, Diadema, SP, Brazil.
  • Caseli L; Instituto de Ciências Ambientais, Químicas e Farmacêuticas, Universidade Federal de São Paulo, UNIFESP, Diadema, SP, Brazil. Electronic address: lcaseli@unifesp.br.
Colloids Surf B Biointerfaces ; 135: 639-645, 2015 Nov 01.
Article em En | MEDLINE | ID: mdl-26322478
Currently, many biological substances extracted from algae have received special attention because of their intrinsic characteristics, which can be applied to different areas of biotechnology. Therefore, in the current study, exopolysaccharides (EPS) from the microalgae Cryptomonas tetrapirenoidosa were employed as an aqueous subphase of a monolayer formed by the lipid dioctadecyldimethylammonium bromide (DODAB). The primary objective of this approach was to evaluate whether EPS could serve as a matrix for the immobilization of the enzyme urease to produce biosensors for urea. After DODAB was spread on the EPS solutions, urease was injected into the aqueous subphase, and the surface was submitted to compression using lateral barriers. The monolayers were subsequently characterized by surface pressure-area isotherms and polarization modulation infrared reflection-absorption spectroscopy (PM-IRRAS). The results indicated that EPS enhanced the adsorption of the enzyme on the lipid monolayer. The mixed films were later transferred to solid supports using the Langmuir-Blodgett (LB) technique and were characterized by transfer ratio, PM-IRRAS, quartz crystal microbalance, and atomic force microscopy. The immobilization of the enzyme on solid supports was fundamental for providing an ideal geometrical accommodation of urease because the interaction of EPS with urease in solution causes a decrease of the relative activity of urease. Therefore, these LB films are promising for the fabrication of future urea biosensors, the architecture of which can be manipulated and enhanced at the molecular level.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Urease / Criptófitas / Enzimas Imobilizadas Idioma: En Revista: Colloids Surf B Biointerfaces Assunto da revista: QUIMICA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Urease / Criptófitas / Enzimas Imobilizadas Idioma: En Revista: Colloids Surf B Biointerfaces Assunto da revista: QUIMICA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda