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

Ramani, K.; Karthikeyan, S.; Boopathy, R.; Kennedy, L. John; Mandal, Asit Baran; Sekaran, G.

doi:10.1016/j.procbio.2011.11.025

Cited by 83 publications

(49 citation statements)

References 86 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lately, mesoporous-activated carbon particles containing large contact sites for enzyme immobilization have been used for immobilizing acid protease and acidic lipases where catalytic efficiency has been significantly maintained after 21 cycles of reuse (Kumar et al 2010; Ramani et al 2011). It was also found that activated carbon with a high surface area (600–1,000 m 2 g −1 ) and a significant fraction of its pore volume in the 300–1,000 Å range was suitable for enzyme immobilization (Daoud et al 2010).…”

Section: Materials Used For Fabrication Of Immobilization Supportsmentioning

confidence: 99%

Enzyme immobilization: an overview on techniques and support materials

2012

View full text Add to dashboard Cite

The current demands of the world’s biotechnological industries are enhancement in enzyme productivity and development of novel techniques for increasing their shelf life. These requirements are inevitable to facilitate large-scale and economic formulation. Enzyme immobilization provides an excellent base for increasing availability of enzyme to the substrate with greater turnover over a considerable period of time. Several natural and synthetic supports have been assessed for their efficiency for enzyme immobilization. Nowadays, immobilized enzymes are preferred over their free counterpart due to their prolonged availability that curtails redundant downstream and purification processes. Future investigations should endeavor at adopting logistic and sensible entrapment techniques along with innovatively modified supports to improve the state of enzyme immobilization and provide new perspectives to the industrial sector.

show abstract

Section: Materials Used For Fabrication Of Immobilization Supportsmentioning

confidence: 99%

Enzyme immobilization: an overview on techniques and support materials

2012

View full text Add to dashboard Cite

show abstract

“…42 The FT-IR spectrum of MICE-FNAC (Fig. The signicant increase in the intensity of the band at 1715.57 cm À1 in FNAC corresponds to C-O stretching vibrations of carbonyl or aldehyde groups.…”

Section: Fourier Transform-infrared Spectroscopic Studies the Ft-ir mentioning

confidence: 99%

Immobilization of thermotolerant intracellular enzymes on functionalized nanoporous activated carbon and application to degradation of an endocrine disruptor: kinetics, isotherm and thermodynamics studies

2015

View full text Add to dashboard Cite

A bacterium, Serratia marcescens capable of degrading the endocrine disruptor, 2-nitrophloroglucinol (NPG) was isolated from tannery wastewater contaminated soil. The mixed intracellular enzymes (MICE) produced from S. marcescens were extracted and characterized. The functionalized nanoporous activated carbon matrix (FNAC) was prepared to immobilize MICE. The optimum conditions for the immobilization of MICE on FNAC were found to be time, 2.5 h; pH, 7.0; temperature, 40 C; concentration of MICE, 4 mg; particle size of FNAC, 300 mm and mass of FNAC, 1 g. The FNAC materials before and after immobilization of MICE were characterized using scanning electron microscopy, Fourier transform-infrared spectrophotometry and an X-ray diffractometer. The thermal behaviour of the free and the immobilized MICE was studied using thermogravimetric analysis. The immobilization of MICE on FNAC obeyed the Freundlich model and the immobilization process followed a pseudo second order kinetic model. MICE-FNAC matrix was used to degrade NPG in aqueous solution. The degradation of NPG by MICE-FNAC was optimum at contact time, 3 h; pH, 7.0; temperature, 40 C; concentration of NPG, 20 mM and agitation speed, 70 rpm. The degradation of NPG was found to be enhanced in the presence of Zn 2+ , Cu 2+ , Ca 2+ and V 3+ ions. The degradation of NPG by MICE-FNAC was studied using UV-visible, fluorescence and FTIR spectroscopy. The degradation of NPG by MICE-FNAC was confirmed using HPLC, NMR and GC-MS spectroscopy. Fig. 9 Degradation of NPG using MICE-FNAC (a) effect of time (experimental conditions: pH, 7; temperature, 30 C; initial NPG concentration, 10 mM; agitation speed, 70 rpm), (b) effect of pH (experimental conditions: time, 3 h; temperature, 30 C; initial NPG concentration, 10 mM; agitation speed, 70 rpm), (c) effect of temperature (experimental conditions: time, 3 h; pH, 7; initial NPG concentration, 10 mM; agitation speed, 70 rpm), (d) effect of initial concentration of NPG (experimental conditions: time, 3 h; pH, 7; temperature, 40 C; agitation speed, 70 rpm) and (e) effect of agitation speed (experimental conditions: time, 3 h; pH, 7; temperature, 40 C; initial NPG concentration, 20 mM). 66250 | RSC Adv., 2015, 5, 66239-66259 This journal isFig. 11 Fluorescence spectra of (a) NPG, (b) NPG degradation using MICE-FNAC in presence of vanadium (c) all metal ions (d) calcium, (e) copper and (f) zinc ions. 66252 | RSC Adv., 2015, 5, 66239-66259 This journal is

show abstract

“…This technique involves the formation of labile Schiff's base interactions due to the reaction between amine and aldehyde groups, leading to the formation of stable secondary amine linkages, whereas the enzyme is immobilized by covalent bonds, due to its high ionic strength . This process is more suitable for materials presenting high porosity and surface area, and good resistance to the functionalization conditions, which can use high temperatures . Biochars (BC) are characterized by these properties, and several studies have evaluated the enzymatic immobilization in BCs from different biomasses such as caja seeds, almond shell and rice husk.…”

Section: Introductionmentioning

confidence: 99%

Pepsin immobilization on biochar by adsorption and covalent binding, and its application for hydrolysis of bovine casein

Santos

Brito

Evaldo

et al. 2019

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND The objective of this research was to compare the efficiency of pepsin immobilization by adsorption and covalent binding on biochar obtained from pupunha palm processing residue, and to use the immobilized enzyme in the hydrolysis of bovine casein. RESULTS The surface modification of biochar with glutaraldehyde was effective, as shown by Fourier transform infrared analyses and the texture properties of the carbons. Both activated and functionalized biochar showed high immobilization efficiency (>95%) and high enzyme‐support binding capacity (>96 mg g–1). During the activity assays, the functionalized carbon showed a higher casein hydrolysis rate when compared to the enzyme immobilized by adsorption, with values of 39.17 U and 32.67 U, respectively, and c. 95% of the activity of the free enzyme, after 60 min. CONCLUSION The functionalization of the biochar led to a surface modification of biochar by the insertion of amine‐aldehyde groups, which was responsible for the formation of strong interactions between the support material and the enzyme, thus providing a greater proteolytic activity when compared to immobilization by adsorption. The immobilized enzymes were able to maintain their proteolytic activity for more than seven cycles of reuse. © 2019 Society of Chemical Industry

show abstract

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

Cited by 83 publications

References 86 publications

Enzyme immobilization: an overview on techniques and support materials

Enzyme immobilization: an overview on techniques and support materials

Immobilization of thermotolerant intracellular enzymes on functionalized nanoporous activated carbon and application to degradation of an endocrine disruptor: kinetics, isotherm and thermodynamics studies

Pepsin immobilization on biochar by adsorption and covalent binding, and its application for hydrolysis of bovine casein

Contact Info

Product

Resources

About