Production of lipase from Geotrichum sp and adsorption studies on affinity resin

Abstract

There is a growing interest in microbial lipase production due to its great potential for industrial applications such as food additives, industrial reagents and stain removers, as well as for medical applications. Specially for medical applications a high degree of purity is required, which is accomplished with high resolution chromatographic techniques. Affinity chromatography is considered a very high resolution chromatographic technique. In this work the adsorption isotherms and kinetics of the adsorption of lipase from Geotrichum sp on biospecific resin were determined. The resin was prepared using EAH sepharose 4B gel (Pharmacia), made to react with oleic acid as the specific ligand.The lipase was produced in a five-liter fermenter, with both complex and synthetic media. Fermentation conditions were a temperature of 30°C, an aeration of 1VVM and an agitation of 400 rpm. Maximum lipase activity was around 28 U/ml after 10 hours of fermentation for the complex medium. The kinetic model and parameters were determined by dynamic fitting to experimental results using the fourth-order Runge-Kutta method

Adsorption of amyloglucosidase from Aspergillus niger NRRL 3122 using ion exchange resin

“…These problems could happen when working with crude broth instead of a system model, because the kinetic assays was made by activity analysis and not by the absorbance reading (280 nm), making it difficult to verify if a denatured enzyme was or wasn't adsorbed by the resin. A similar situation was observed by Kamimura et al (1999), where the value of Q m obtained in the kinetic curves was inferior to the isotherm and when the recovered resin was used, the capacity of adsorption decreased strongly. However, the decrease in the adsorption efficiency for the recovered resins suggested that the regeneration step should be studied carefully in order to improve it.…”

Effects of process variables and additives on mustard oil hydrolysis by porcine pancreas lipase

“…At oil-water interface, it hydrolyzes carboxyl ester bond to release fatty acids and organic alcohols (Pereira et al, 2003;Leal et al, 2002;Kamimura et al, 1999;Merçon et al, 1997). In comparison with the aforementioned processes, lipase catalyzed hydrolysis has distinct advantages of excellent product purity and mild process conditions (normal pressure and nearly ambient temperature).…”

Seed lipases: sources, applications and properties - a review

“…The participation of lipases in the worldwide enzyme industry market has grown significantly and it is believed that, in the future, they will acquire importance comparable to that of the peptidases, which currently represent 25 to 40% of industrial enzyme sales (Hasan et al 2006). Lipases act, by definition, at the organic-aqueous interface, catalyzing the hydrolysis of estercarboxylate bonds and releasing fatty acids and organic alcohols (Pereira et al, 2003;Leal et al 2002;Kamimura et al, 1999;Merçon et al 1997). However, as Pottevin showed for the first time in 1906, in water-restricted environments, the reverse reaction (esterification) or even various transesterification reactions can occur Castilho 2008, Castro et al 2000).…”