Mesoporous activated carbon (MAC) derived from rice husk is used for the immobilization of acidic lipase (ALIP) produced from Pseudomonas gessardii. The purified acidic lipase had the specific activity and molecular weight of 1473 U/mg and 94 kDa respectively. To determine the optimum conditions for the immobilization of lipase onto MAC, the experiments were carried out by varying the time (10-180 min), pH (2-8), temperature (10-50 °C) and the initial lipase activity (49 × 103, 98 × 103, 147 × 103 and 196 × 103 U/l in acetate buffer). The optimum conditions for immobilization of acidic lipase were found to be: time-120 min; pH 3.5; temperature-30 °C, which resulted in achieving a maximum immobilization of 1834 U/g. The thermal stability of the immobilized lipase was comparatively higher than that in its free form. The free and immobilized enzyme kinetic parameters (Km and Vmax) were found using Michaelis-Menten enzyme kinetics. The Km values for free enzyme and immobilized one were 0.655 and 0.243 mM respectively. The immobilization of acidic lipase onto MAC was confirmed using Fourier Transform-Infrared Spectroscopy, X-ray diffraction analysis and scanning electron microscopy. © 2009 Elsevier B.V. All rights reserved.

John Kennedy L

Physics

School of Advanced Sciences

Chennai Campus

Vidya R

VIT School for Agricultural Innovations and Advanced Learning

Vellore Campus

Kandasamy R

Boopathy R

Sekaran G.

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

&nbsp;

&nbsp;

VIT University

Journal of Molecular Catalysis B: Enzymatic

This study deals with the surface functionalization of mesoporous activated carbon, using ethylenediamine and glutaraldehyde to facilitate the strong immobilization of acidic lipase (AL) onto MAC. The AL was produced from Pseudomonas gessardii by using slaughterhouse lipid waste as the substrate. The AL immobilized on functionalized mesoporous activated carbon (ALFMAC) was applied for the hydrolysis of waste cooked oil (WCO). The optimum conditions for the immobilization of AL onto functionalized mesoporous activated carbon (FMAC) were 90 min; pH 3.5; and 35 °C; which resulted at the maximum immobilization of 5440 U/g of FMAC (3.693 mg of AL/g of FMAC or the yield 2.7% or the expressed activity 103.7% or the activity per unit area of FMAC 1.08 mg of AL/m 2). The ALFMAC showed better thermal and storage stabilities than the free AL. The ALFMAC retained a 98% and a 92% initial activity at 40 °C and 50 °C, respectively, while the AL showed the thermal stability (residual activities) 65% and 38%, respectively. The storage stability of ALFMAC at 4 °C showed 100% initial activity up to 15 days from the initial day of the storage, whereas AL showed only 88% initial activity up to 15 days. The FMAC and ALFMAC were characterized by using scanning electron microscopy (SEM), Fourier transform infrared (FT-IR) spectroscopy, and X-ray diffraction (XRD) analysis. The K m values of the ALFMAC and AL were 0.112 mM and 0.411 mM, respectively. The v max values of the ALFMAC and AL were 1.26 mM/min and 0.53 mM/min, respectively. Immobilization of AL onto FMAC obeyed the Freundlich and Redlich-Peterson isotherm models. The non-linear models of pseudo first, and second order, intra-particle diffusion, Bangham, and Boyd plot were also performed to understand the dynamic mechanism of immobilization. ALFMAC showed a 100% hydrolysis of WCO up to 21 cycles of reuse, and 60% up to 45 cycles. The hydrolysis of WCO was confirmed by using FT-IR spectra. © 2011 Elsevier Ltd. All rights reserved.

Process Biochemistry

Surface functionalized mesoporous activated carbon for the immobilization of acidic lipase and their application to hydrolysis of waste cooked oil: Isotherm and kinetic studies

Journal of Environmental Biology

Analysis of genetic diversity in Indian and exotic linseed germplasm and identification of trait specific superior accessions

International Journal of Biological Macromolecules

Immobilization of Candida rugosa lipase on sporopollenin from Lycopodium clavatum

Characterization of the lipase immobilized on Mg–Al hydrotalcite for biodiesel

Applied Clay Science

Enzyme immobilizationPart 1. Modified bentonite as a new and efficient support for immobilization of Candida rugosa lipase

Bioresource Technology

Immobilization of lipase on methyl-modified silica aerogels by physical adsorption

Immobilization of acidic lipase derived from Pseudomonas gessardii onto mesoporous activated carbon for the hydrolysis of olive oil

Journal	Data powered by TypesetJournal of Molecular Catalysis B: Enzymatic
Publisher	Data powered by TypesetElsevier BV
ISSN	1381-1177
Open Access	No