Preparation and Characterization of Cellulose Triacetate as Support for Lecitase Ultra Immobilization

Abstract

The use of polymers as supports for enzyme immobilization is a strategy that enables to remove the enzymes from a chemical reaction and improve their efficiency in catalytic processes. In this work, cellulose triacetate (CTA) was used for physical adsorption of phospholipase Lecitase ultra (LU). CTA is more hydrophobic than cellulose, shows good performance in the lipases immobilization being a good candidate for immobilization of phospholipases. We investigated the immobilization of LU in CTA, the stability of the immobilized enzyme (CTA-LU) and the performance of CTA-LU using soybean oil as a substrate. LU was efficiently immobilized in CTA reaching 97.1% in 60 min of contact with an enzymatic activity of 975.8 U·g−1. The CTA-LU system presents good thermal stability, being superior of the free enzyme and increase of the catalytic activity in the whole range of pH values. The difference observed for immobilized enzyme compared to free one occurs because of the interaction between the enzyme and the polymer, which stabilizes the enzyme. The CTA-LU system was used in the transesterification of soybean oil with methanol, with the production of fatty acid methyl esters. The results showed that CTA-LU is a promising system for enzymatic reactions.

Suitability of Immobilized Systems for Microbiological Degradation of Endocrine Disrupting Compounds

“…CTA presents a great balance of the hydrophilic/hydrophobic character important for effective enzyme adsorption and its biological activity. Additionally, hydrophilic/hydrophobic properties could be modified by acetylation/deacetylation [ 69 ]. Both strains were able to degrade 2 mg/L of estrone and 17β-estradiol for free strains in 24 h and for immobilized in 72 h, which is probably caused by the compounds transfer limitation in a porous carrier.…”

“…Both strains were able to degrade 2 mg/L of estrone and 17β-estradiol for free strains in 24 h and for immobilized in 72 h, which is probably caused by the compounds transfer limitation in a porous carrier. Additionally, the authors reported that a continuous-flow degradation on an IBRC reactor of 850 ng/L 17β-estradiol is possible [ 69 ].…”

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

“…However, in many cases, it is also related with a decrease in enzyme activity caused by various types of distortion, diffusion, and steric problems [46]. As Lecitase™ Ultra is commercially available only in its free form as the water solution, many attempts have been made to prepare an immobilized form of this enzyme for different purposes, for example, by entrapment in gelatin hydrogel [47] or in different calcium alginates [48], immobilization on the derivatives of cellulose [49,50], polystyrene resin [51], styrene-divinylbenzene beads [37,52], magnetic nanoparticles [53], or by encapsulation in AOT(bis(2-ethylhexyl) sulfosuccinate sodium salt)/isooctane reverse micelles [54]. In the processes of the kinetic resolution of racemates catalyzed by immobilized Lecitase™ Ultra, the best results were obtained using gelatin [35,39], various derivatives of agarose [33,36,38,41,55], hexyl-and butyl-toyopearl [34], or epoxy activated polymer Dilbead VWR coated with polyethylenimine (PEI) and crosslinked with glutaraldehyde [40].…”

Enantioselective Transesterification of Allyl Alcohols with (E)-4-Arylbut-3-en-2-ol Motif by Immobilized Lecitase™ Ultra

“…Immobilization of enzymes by adsorption is one of the oldest and also the most frequently used methods due to the relatively low costs and simple procedure. LU adsorbed physically on cellulose triacetate was used for the production of fatty acid methyl esters from soybean oil by transesterification [43]. Adsorption of LU on different ionic and macropourous resins found applications in lipid chemistry, including acidolysis of phospholipids [28,44,45], glycerolysis of soybean oil [46], esterification of glycerol with oleic acid [47], hydrolysis of phosphatidylcholine to lysophosphatidylcholine [48], and esterification of isopropylidene glycerol in the production of monoacylglycerols [49].…”