Immobilization of Candida antarctica lipase B by adsorption to green coconut fiber.

Appl Biochem Biotechnol

Escola de Química, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.

Published: March 2008

AI Article Synopsis

  • An agroindustrial byproduct, green coconut fiber, was tested for its effectiveness in immobilizing CALB lipase through physical adsorption.
  • Various factors influencing the immobilization process such as contact time, enzyme concentration, and pH were examined to optimize the method.
  • The immobilized CALB exhibited significantly improved thermal stability and maintained operational stability in synthesizing butyl butyrate, although it showed lower activity retention compared to Novozyme 435 in hydrolysis after multiple cycles.

Article Abstract

An agroindustrial residue, green coconut fiber, was evaluated as support for immobilization of Candida antarctica type B (CALB) lipase by physical adsorption. The influence of several parameters, such as contact time, amount of enzyme offered to immobilization, and pH of lipase solution was analyzed to select a suitable immobilization protocol. Kinetic constants of soluble and immobilized lipases were assayed. Thermal and operational stability of the immobilized enzyme, obtained after 2 h of contact between coconut fiber and enzyme solution, containing 40 U/ml in 25 mM sodium phosphate buffer pH 7, were determined. CALB immobilization by adsorption on coconut fiber promoted an increase in thermal stability at 50 and 60 degrees C, as half-lives (t (1/2)) of the immobilized enzyme were, respectively, 2- and 92-fold higher than the ones for soluble enzyme. Furthermore, operational stabilities of methyl butyrate hydrolysis and butyl butyrate synthesis were evaluated. After the third cycle of methyl butyrate hydrolysis, it retained less than 50% of the initial activity, while Novozyme 435 retained more than 70% after the tenth cycle. However, in the synthesis of butyl butyrate, CALB immobilized on coconut fiber showed a good operational stability when compared to Novozyme 435, retaining 80% of its initial activity after the sixth cycle of reaction.

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http://dx.doi.org/10.1007/s12010-007-8072-4DOI Listing

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