Abstract
Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized by covalent binding with epichlorohydrin without (203%) and with PIL (250%), was assessed by the following the hydrolysis reaction of olive oil and characterized biochemically (Michaelis–Menten constant, optimum pH and temperature, and operational stability). Further, the potential transesterification activity for three substrates: sunflower, soybean, and colza oils, was also determined, achieving a conversion of ethyl esters between 70 and 98%. The supports and the immobilized lipase systems were characterized using Fourier transform infrared spectra (FTIR), scanning electron microscopy (SEM), elemental analysis, and thermogravimetric (TG) analysis.
Highlights
Free or immobilized lipases are the most studied class of enzymes in biotechnology, receiving attention both in academia and in industry because of the recent improvement in biocatalytic enzyme performance [1,2,3]
The activity recovery yield of the two preparations of immobilized lipase by covalent binding onto silica xerogel supports obtained by a sol-gel technique treated (SIL) or no (SC) with ionic liquid and epichlorohydrin (CBE) or glutaraldehyde (CBG) was investigated using an olive oil hydrolysis reaction as a model [13,26,27,28]
Surface treated silica supports were used to immobilize the lipase from Burkholderia cepacia by covalent binding
Summary
Free or immobilized lipases are the most studied class of enzymes in biotechnology, receiving attention both in academia and in industry because of the recent improvement in biocatalytic enzyme performance [1,2,3]. Transesterification using LBC has been reported by several studies and with different oils: soybean [5], palm [6], cotton seed [7], jatropha [8], sunflowers [9], and colza [10]. The use of an appropriate support can influence the biocatalyst physical-chemical properties, such as diffusion and catalytic efficiency on each specific reaction system [15,16]. Direct investigation of what occurs concerning the catalytic efficiency, morphology and physical chemistry, is quite a formidable task, and the differences observed in the performance of the immobilized enzyme system must be interpreted very carefully. In any study dealing with enzyme immobilization, the prerequisite is rigorous planning and reporting of experiments [17]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
