Regioselective enzymatic hydrolysis of hexa-O-acetyl-lactal in a green non-aqueous medium

Bavaro, Teodora; Torres‐Salas, Pamela; Ubiali, Daniela; Terreni, Marco

doi:10.1039/c3ra40266e

Cited by 10 publications

(6 citation statements)

References 26 publications

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“…Sugars are hardly solubilized in organic solvents, such as tert -butyl alcohol [ 49 , 50 ]. The addition of small amounts of water could to increase the fructose solubility in the reaction medium and to prevent the enzyme inactivation.…”

Section: Resultsmentioning

confidence: 99%

Immobilized Lipases on Functionalized Silica Particles as Potential Biocatalysts for the Synthesis of Fructose Oleate in an Organic Solvent/Water System

et al. 2017

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Lipases from Thermomyces lanuginosus (TLL) and Pseudomonas fluorescens (PFL) were immobilized on functionalized silica particles aiming their use in the synthesis of fructose oleate in a tert-butyl alcohol/water system. Silica particles were chemically modified with octyl (OS), octyl plus glutaraldehyde (OSGlu), octyl plus glyoxyl (OSGlx), and octyl plus epoxy groups (OSEpx). PFL was hyperactivated on all functionalized supports (more than 100% recovered activity) using low protein loading (1 mg/g), however, for TLL, this phenomenon was observed only using octyl-silica (OS). All prepared biocatalysts exhibited high stability by incubating in tert-butyl alcohol (half-lives around 50 h at 65 °C). The biocatalysts prepared using OS and OSGlu as supports showed excellent performance in the synthesis of fructose oleate. High ester synthesis was observed when a small amount of water (1%, v/v) was added to the organic phase, allowing an ester productivity until five times (0.88–0.96 g/L.h) higher than in the absence of water (0.18–0.34 g/L.h) under fixed enzyme concentration (0.51 IU/g of solvent). Maximum ester productivity (16.1–18.1 g/L.h) was achieved for 30 min of reaction catalyzed by immobilized lipases on OS and OSGlu at 8.4 IU/mL of solvent. Operational stability tests showed satisfactory stability after four consecutive cycles of reaction.

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Section: Resultsmentioning

confidence: 99%

Immobilized Lipases on Functionalized Silica Particles as Potential Biocatalysts for the Synthesis of Fructose Oleate in an Organic Solvent/Water System

et al. 2017

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“…tert ‐Butanol has been recently reported by some of the Authors as an efficient low‐water medium for lipase‐mediated hydrolyses of peracetylated disaccharides. Moreover, the limited amount of water in the medium can assist in the control of enzyme selectivity . In the case of hempseed oil hydrolysis, as expected, such a medium dramatically enhanced the solubility of acylglycerols giving a homogeneous solution where water does not play the role of solvent but acts as the necessary reagent to carry out the hydrolysis.…”

Section: Resultsmentioning

confidence: 80%

Preparation of PUFA concentrates as acylglycerols via enzymatic hydrolysis of hempseed oil (Cannabis sativa L.) in a homogeneous low‐water medium

Torres‐Salas

Pedrali

Bavaro

et al. 2014

Euro J Lipid Sci & Tech

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The growing demand for concentrated extracts of PUFA prompted us to undertake the preparation of natural glycerides containing linoleic acid and a-linolenic acid from hempseed oil. Hempseed is an exceptionally rich source of essential FA but is still underutilized. Hempseed oil was thus submitted to a lipase-catalyzed hydrolysis in a homogeneous medium based on oil and t-BuOH/water. Seven commercial lipases were screened in this reaction medium, which resulted to be superior to the routinely used biphasic systems in terms of substrate/product solubility and biocatalyst stability. Lipase from Pseudomonas cepacia resulted to be sufficiently selective versus saturated FA and it was thus used to hydrolyze hempseed oil in order to obtain acylglycerols enriched with PUFA. The enzymatic reaction was scaled up and the acylglycerol components were purified and analyzed by GC-FID. In the fraction of monoacylglycerols (yield 22%) the total amount of PUFA reached 85% (against 77% of the crude oil) whereas the content of saturated FA was negligible. The omega-6/omega-3 ratio of the total glyceride component (purified acylglycerols, yield 29%) was maintained in the optimal range (4.6:1) for human nutrition. Therefore, PUFA concentrates from hempseed oil here obtained in the form of natural glycerides could be considered as valuable dietary supplements.Practical applications: The enzymatic method here described allows to directly achieve pure monoglycerides of PUFA with a potential nutraceutical use. This procedure has the advantage to occur under very mild conditions in a homogeneous medium composed of a water miscible green solvent, to be easily scalable and to rely on a standard chromatography purification step.

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“…The biocatalytic use of enzymes provides the possibility to develop efficient processes with low environmental impact in several fields ranging from pharma to food [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16]. Nowadays, covalent immobilization of enzymes [17][18][19] is increasingly used to improve operational performances, to ensure the recovery and the reuse of the biocatalysts and to avoid contamination of the final product with residual proteins [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications

et al. 2019

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In this paper, we describe the development of an efficient enzyme immobilization procedure based on the activation of epoxy carriers with glucosamine. This approach aims at both creating a hydrophilic microenvironment surrounding the biocatalyst and introducing a spacer bearing an aldehyde group for covalent attachment. First, the immobilization study was carried out using penicillin G acylase (PGA) from Escherichia coli as a model enzyme. PGA immobilized on glucosamine activated supports has been compared with enzyme derivatives obtained by direct immobilization on the same non-modified carriers, in the synthesis of different 3′-functionalized cephalosporins. The derivatives prepared by immobilization of PGA on the glucosamine-carriers performed better than those prepared using the unmodified carriers (i.e., 90% versus 79% cefazolin conversion). The same immobilization method has been then applied to the immobilization of two other hydrolases (neutral protease from Bacillus subtilis, PN, and bromelain from pineapple stem, BR) and one transferase (γ-glutamyl transpeptidase from Bacillus subtilis, GGT). Immobilized PN and BR have been exploited in the synthesis of modified nucleosides and in a bench-scale packed-bed reactor for the protein stabilization of a Sauvignon blanc wine, respectively. In addition, in these cases, the new enzyme derivatives provided improved results compared to those previously described.

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Regioselective enzymatic hydrolysis of hexa-O-acetyl-lactal in a green non-aqueous medium

Cited by 10 publications

References 26 publications

Immobilized Lipases on Functionalized Silica Particles as Potential Biocatalysts for the Synthesis of Fructose Oleate in an Organic Solvent/Water System

Immobilized Lipases on Functionalized Silica Particles as Potential Biocatalysts for the Synthesis of Fructose Oleate in an Organic Solvent/Water System

Preparation of PUFA concentrates as acylglycerols via enzymatic hydrolysis of hempseed oil (Cannabis sativa L.) in a homogeneous low‐water medium

Developing a Novel Enzyme Immobilization Process by Activation of Epoxy Carriers with Glucosamine for Pharmaceutical and Food Applications

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