Immobilization of Candida cylindracea lipase on poly lactic acid, polyvinyl alcohol and chitosan based ternary blend film: Characterization, activity, stability and its application for N-acylation reactions

Badgujar, Kirtikumar C.; Dhake, Kishor P.; Bhanage, Bhalchandra M.

doi:10.1016/j.procbio.2013.06.009

Cited by 87 publications

(78 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…lipases have extensively been immobilized on diversified materials such as pretreated textile (Adachi et al 2006); nonwoven fabrics of polypropylene, polyethylene terephthalate, and viscose fiber ; macroporous silica monoliths ; silica-PEG gel (Yang et al 2010); treated chitosan membranes (Orrego et al 2010); ternary blend film comprising of chitosan, polylactic acid (PLA), and polyvinyl alcohol (Badgujar et al 2013); chitosan tethered poly(acrylonitrile-co-maleic acid) surface (Ye et al 2005); natural kaolin (Rahman et al 2005a, b); and Amberlite IRC-50 and Al 2 O 3 (Minovska et al 2005). Immobilization of R. oryzae lipase on silica aerogels (Kharrat et al 2011), and Thermomyces sp.…”

Section: Lipase Immobilizationmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

View full text Add to dashboard Cite

Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

show abstract

Section: Lipase Immobilizationmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

View full text Add to dashboard Cite

show abstract

“…To overcome the above said drawbacks, there is a need to use an efficient catalytic system which can be operated under mild conditions and provide significant % yield of corresponding valuable levulinate products with greener loom [1,2,8,9]. More recently, the American Chemical Society Green Chemistry Institute (ACS-GCI) was established to promote innovations in the synthesis of precious molecules by using sustainable green chemistry and technology [14].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover protocol is recyclable and can be called "natural" [17]. Additionally enzymes are the "energy saving" catalyst, since enzyme catalysts require less energy for activation as compared to traditional chemical catalysts [14,16]. Moreover, the enzyme catalyzed reactions are selective, hence avoiding the side waste (impurity) formation/treatment and consequently reducing the E-factor; which ultimately improve the reaction % yield and mass efficiency [13,15].…”

Section: Introductionmentioning

confidence: 99%

Thermo-chemical energy assessment for production of energy-rich fuel additive compounds by using levulinic acid and immobilized lipase

Badgujar

Bhanage

2015

Fuel Processing Technology

Self Cite

View full text Add to dashboard Cite

“…The possible reasons of the enhanced activity of immobilized lipase are as follow: (i) maintenance of "open state" conformation of lipase due to immobilization; [40][41][42] (ii) prevention of aggregation of free lipase due to immobilization; 17,43 and (iii) change in enzyme conformation due to interfacial activation. 41,44 Either one or all might be possible for enhanced activity. It suggests that covalent binding of lipase to AuNPs-NH 2 might have occurred at such sites that facilitated the easy accessibility of substrate to the catalytic sites by keeping its active conformation open, leading to significant increase in catalytic efficiency.…”

Section: Enzyme Kinetics Measurementmentioning

confidence: 99%

Facile fabrication of lipase to amine functionalized gold nanoparticles to enhance stability and activity

2017

View full text Add to dashboard Cite

Among various techniques of immobilization, EDC/NHS cross linking is a simple and single step process for covalent coupling between enzymes and nanoparticles. Here we describe immobilization of lipase on amine functionalized gold nanoparticles (AuNPs-NH 2 ) to attain enhanced activity and stability. To achieve a suitable orientation, it is necessary to understand the contribution of different functional groups on the enzyme's surface. Therefore, the crystal structure of lipase was analyzed using a computational method (PyMOL) to find the exposed acidic amino acid residues that can be exploited for conjugation. Confirmation of conjugation (AuNP-NH 2 -lipase) was determined by various techniques such as agarose gel electrophoresis, zeta measurement, FTIR-spectroscopy and TEM. Further, catalytic parameters (V max , K M,app , K cat , and K cat /K M,app ) have been studied to establish activity enhancement upon immobilization. The data also suggested that, AuNP-NH 2 -lipase has desirable improved parameters such as temperature and storage stability. The thermodynamic parameters for the kinetics of deactivation IntroductionEnzymes have wide application in food, detergent, medicine, diagnostics, energy and many other industrial sectors due to their catalytic activity under mild conditions, specicity, costeffectiveness and greener production conditions. 1,2 However industrial application of free enzymes is restricted due to high lability, poor stability and problems in their recovery and reuse. 3Immobilization is the effective way to overcome these limitations and extend the horizon of their applications.4 Various methods of immobilization include physical adsorption, ionic interaction, covalent bonding between support and enzyme or entrapment within the different matrices.5 Hydrophobic interactions, ionic interactions, hydrogen bonds, van der Waals interactions and solvation are the major forces responsible for non-covalent interactions. Except for covalent attachment, the above mentioned techniques mainly rely on weak interactions, therefore enzymes are prone to detachment from the support surface with time. Covalent bonding mediated immobilization helps in improving enzyme activity at the cost of loss of conformational integrity.6 A very simple method of crosslinking biomolecules to nanoparticles relies on EDC/NHS coupling in which carbodiimides mediate formation of amide bond between carboxy and amine groups.7 High solubility in water, ease to remove byproducts, zero length cross linking molecule and single step reaction provides an edge over other methods in EDC/NHS coupling.8 Several enzymes have been conjugated using this strategy, but they lack in their structure based consideration prior to immobilization. Improper orientation aer immobilization ultimately affects activity; therefore, it is highly essential to understand the structure of protein before immobilization. One of the rationale approaches is to exploit specic surface amino acids for conjugating enzymes with the nanosurface so that the catalytic p...

show abstract

Immobilization of Candida cylindracea lipase on poly lactic acid, polyvinyl alcohol and chitosan based ternary blend film: Characterization, activity, stability and its application for N-acylation reactions

Cited by 87 publications

References 55 publications

An insight into microbial lipases and their environmental facet

An insight into microbial lipases and their environmental facet

Thermo-chemical energy assessment for production of energy-rich fuel additive compounds by using levulinic acid and immobilized lipase

Facile fabrication of lipase to amine functionalized gold nanoparticles to enhance stability and activity

Contact Info

Product

Resources

About