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Siham Akmoussi-Toumi, Souad Khemili-Talbi, Imen Ferioune, Salima Kebbouche-Gana
The present study investigates the purification and biochemical characterization of an extracellular lipase (HML) from Haloarchaea Haloferax mediterranei strain ATS1, isolated from the Sebkha (Medea, Algeria). The pure protein was obtained with ammonium sulfate precipitation (40-70%)-dialysis and UNO Q-6 FPLC, and characterized biochemically. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme was a monomer, with a molecular mass of 45,011...
May 15, 2018: International Journal of Biological Macromolecules
Anita Šalić, Ana Jurinjak Tušek, Aleksandra Sander, Bruno Zelić
Although the application of microreactors in different processes has been extensively explored in recent decades, microreactors continue to be underexplored in the context of the enzyme-catalysed process for biodiesel production. Due to their numerous advantages, microreactors could become the next step in the development of a biodiesel production process characterised by sustainability, cost-effectiveness and energy efficiency. In this investigation, biodiesel production was catalysed by lipase from Thermomyces lanuginosus (Lipolase L100)...
February 5, 2018: New Biotechnology
Efstratios Nikolaivits, Aikaterini Termentzi, Alexios-Leandros Skaltsounis, Nikolas Fokialakis, Evangelos Topakas
Oleuropein, a bioactive compound found in all parts of olive tree, especially in leaves and branches, presents numerous health promoting properties that increase research and market interest the last few years. In addition, oleuropein degradation products, such as hydroxytyrosol, elenolic acid, and the aglycones also exhibit biological activities with different properties compared to the starting compound. Under this view, a commercial lipase preparation Lipolase 100L and a thermophilic β-glucosidase from Myceliophthora thermophila were used for the regioselective hydrolysis of oleuropein towards the production of the corresponding biologically active compounds...
July 10, 2017: Journal of Biotechnology
Shivika Sharma, Kriti Kanwar, Shamsher S Kanwar
Ascorbyl palmitate was synthesized using a Celite-immobilized commercial lipase (Lipolase 100L) in dimethylsulfoxide (DMSO) as an organic solvent system. Lipase immobilized by surface adsorption onto Celite 545 matrix and subsequently exposed to 1 % glutaraldehyde showed 75 % binding of protein. The Celite-bound lipase was optimally active at 75 °C and pH 8.5 under shaking and showed maximum hydrolytic activity toward p-NPP as a substrate. The bound lipase was found to be stimulated only in the presence of Al(3+) and EDTA...
December 2016: 3 Biotech
Sara Melis, Anneleen Pauly, Lien R Gerits, Bram Pareyt, Jan A Delcour
Three lipases with different hydrolysis specificities were tested in a laboratory-scale dough-batter wheat flour separation process in two concentrations. Lipolase specifically hydrolyzed nonpolar flour lipids. At the highest concentration tested, it significantly improved gluten agglomeration and yield, also when combined with a xylanase with hydrolysis specificity toward water-extractable arabinoxylan. We hypothesize that its action is due to the release of adequate levels of free fatty acids, which, because at least a part of them is dissociated, act as anionic surfactants...
March 8, 2017: Journal of Agricultural and Food Chemistry
Arti Kumari, Razi Ahmad, Sangeeta Negi, Sunil Kumar Khare
The aim of present work was to effectively remediate grease waste by Penicillium chrysogenum. For efficient degradation, grease waste was pre-treated using various lipases, among them lipolase was the best. The pretreated grease was used as a substrate by P. chrysogenum resulting into the production of fatty acids. Process was optimized by response surface methodology (RSM) using four variables viz; FeCl2 (mM), spore concentration (spores/ml), time period (days) and amount of grease (g). The optimized conditions viz; FeCl2 1...
February 2017: Bioresource Technology
Mathilde S Piel, Günther H J Peters, Jesper Brask
Phospholipases are ubiquitous in nature and the target of significant research aiming at both their physiological roles and technical applications in e.g. the food industry. In the search for sensitive and selective phospholipase assays, we have focused on synthetic FRET (Förster resonance energy transfer) substrates. This has led to the development of a facile, easily scalable and low cost synthesis of fluorogenic phospholipids featuring the dansyl/dabcyl fluorophore/quencher-pair on the fatty acid ω-position and on the phosphatidylethanolamine head group, respectively...
January 2017: Chemistry and Physics of Lipids
Peter Kis, Elena Potocká, Vladimír Mastihuba, Mária Mastihubová
4-Nitrophenyl β-d-apiofuranoside as a chromogenic probe for detection of β-d-apiofuranosidase activity was prepared in 61% yield from 2,3-isopropylidene-α,β-d-apiofuranose through a sequence of five reactions. The synthesis involves one regioselective enzymatic step-benzoylation of primary hydroxyl of 2,3-isopropylidene-α,β-d-apiofuranose catalysed by Lipolase 100T and stereoselective β-d-apiofuranosylation of p-nitrophenol using BF3⋅OEt2/Et3N. The product was used for screening of β-d-apiofuranosidase activity in 61 samples of crude commercial enzymes and plant materials...
July 22, 2016: Carbohydrate Research
Chema Borchani, Fabienne Fonteyn, Guilhem Jamin, Michel Paquot, Philippe Thonart, Christophe Blecker
The yeast cell wall of Saccharomyces cerevisiae is an important source of β-d-glucan, a glucose homopolymer with many functional, nutritional and human health benefits. In the present study, the yeast cell wall fractionation process involving enzymatic treatments (savinase and lipolase enzymes) affected most of the physical and functional characteristics of extracted fractions. Thus, the fractionation process showed that β-d-glucan fraction F4 had significantly higher swelling power and fat binding capacity compared to other fractions (F1, F2 and F3)...
March 1, 2016: Food Chemistry
Adi Dror, Margarita Kanteev, Irit Kagan, Shalev Gihaz, Anat Shahar, Ayelet Fishman
Enzymatic production of biodiesel by transesterification of triglycerides and alcohol, catalyzed by lipases, offers an environmentally friendly and efficient alternative to the chemically catalyzed process while using low-grade feedstocks. Methanol is utilized frequently as the alcohol in the reaction due to its reactivity and low cost. However, one of the major drawbacks of the enzymatic system is the presence of high methanol concentrations which leads to methanol-induced unfolding and inactivation of the biocatalyst...
November 2015: Applied Microbiology and Biotechnology
Xiao-Jun Li, Ren-Chao Zheng, Hong-Ye Ma, Jian-Feng Huang, Yu-Guo Zheng
The variant Lip-T (S88T/A99N/V116D) of lipase Lip from Thermomyces lanuginosus has been proved to be a potential biocatalyst for kinetic resolution of 2-carboxyethyl-3-cyano-5-methylhexanoic acid ethyl ester (CNDE) to produce valuable chiral intermediate of Pregabalin. In this study, random, site-directed and site-saturation mutagenesis were performed to further enhance the activity of Lip-T, and the key residues responsible for catalytic efficiency were revealed. A mutant S63L/D232A with improved activity toward CNDE was obtained after screening of approximately 2500 clones from random-mutant libraries...
October 20, 2014: Journal of Biotechnology
Adriano A Mendes, Heizir F de Castro, Raquel L C Giordano
The aim of this work was to prepare biocatalysts to catalyze the synthesis of butyl butyrate by esterification reaction, and the synthesis of biodiesel by transesterification of palm and babassu oils with ethanol. Lipase preparations Lipolase® (TLL1) and Lipex® 100 L (TLL2) from Thermomyces lanuginosus and Lipase AK from Pseudomonas fluorescens (PFL) were immobilized on glyoxyl-agarose beads prepared by activation with glycidol (Gly) and epichlorohydrin (Epi). The influence of immobilization time, lipase source and activating agents on the catalytic activity of the biocatalysts were evaluated in both aqueous and organic media...
September 2014: International Journal of Biological Macromolecules
Mária Mastihubová, Vladimír Mastihuba
Methyl α-D-glucopyranoside as a model acceptor was acylated by several phenolic and non-phenolic vinyl esters using immobilised Lipolase. Donor specificity and regioselectivity of reaction were investigated. Conversion and rate of acylation by structurally varied donors indicates that the synthetic reactivity of Lipolase corresponds to the hydrolytic activity of feruloyl esterase type A. Lipolase exhibited remarkable regioselectivity for primary position of methyl α-D-glucopyranoside. The acylation occurred exclusively at 6-O primary position when vinyl esters of phenolic acids (hydroxybenzoates, hydroxyphenylalkanoates and hydroxycinnamates) served as acyl donors (5-77%)...
October 1, 2013: Bioorganic & Medicinal Chemistry Letters
Shamsher Singh Kanwar, Rajeev Kumar Kaushal, Arshad Jawed, Reena Gupta, Swapandeep Singh Chimni
A comparative study of various treatments for inhibition of the residual activity of a lipase (obtained from Bacillus coagulans MTCC-6375) in a colorimetric assay using p-nitrophenyl palmitate (pNPP) was made. Direct chilling of contents of reaction mixture or addition of chilled mixture of ethanol : acetone (1:1) decreased the residual lipase activity by 94.0 and 95.0% respectively, as compared to lipase incubated at 45 degrees C for 20 min (control). Amongst various ionic and non-ionic detergents, Triton X-100 (0...
August 2005: Indian Journal of Biochemistry & Biophysics
Debajyoti Goswami, Jayanta Kumar Basu, Sirshendu De
Lipase (triacylglycerol acylhydrolase) is a unique enzyme which can catalyze various types of reactions such as hydrolysis, esterification, alcoholysis etc. In particular, hydrolysis of vegetable oil with lipase as a catalyst is widely studied. Free lipase, lipase immobilized on suitable support, lipase encapsulated in a reverse micelle and lipase immobilized on a suitable membrane to be used in membrane reactor are the most common ways of employing lipase in oil hydrolysis. Castor oil is a unique vegetable oil as it contains high amounts (90%) of a hydroxy monounsaturated fatty acid named ricinoleic acid...
March 2013: Critical Reviews in Biotechnology
Ines Belhaj-Ben Romdhane, Fakher Frikha, Inès Maalej-Achouri, Ali Gargouri, Hafedh Belghith
A genomic bank from Talaromyces thermophilus fungus was constructed and screened using a previously isolated fragment lipase gene as probe. From several clones isolated, the nucleotide sequence of the lipase gene (TTL gene) was completed and sequenced. The TTL coding gene consists of an open reading frame (ORF) of 1083bp encoding a protein of 269 Aa with an estimated molecular mass of 30kDa. The TTL belongs to the same gene family as Thermomyces lanuginosus lipase (TLL, Lipolase®), a well known lipase with multiple applications...
February 15, 2012: Gene
M G Onesti, P Fioramonti, S Carella, G Spinelli, N Scuderi
Active antiretroviral therapy has reduced the mortality of patients with acquired immune deficiency syndrome (AIDS) and increased both the quality of life and the longevity of patients infected with human immunodeficiency virus (HIV). The long-term effects of HIV infection are increasingly observed, particularly changes in fat distribution or "lipodystrophy." Strategies to prevent, mitigate, or reverse HIV-associated lipodystrophy have been difficult to develop. The medical management of fat redistribution usually is ineffective, and surgical approaches to HIV-associated lipodystrophy have already been described, but major drawbacks include recurrence of the fat accumulation...
August 2010: Aesthetic Plastic Surgery
G E Crooks, G D Rees, B H Robinson, M Svensson, G R Stephenson
Humicola lanuginosa lipase (HIL) and Rhizomucor miehei lipase (RrnL), isolated from commercial preparations of Lipolase and Lipozyme, respectively, were solubilized in AOT-stabilized water-in-oil (w/o) microemulsions in n-heptane and aspects of their hydrolysis and condensation activity examined. The temperature dependence of HIL hydrolysis activity in unbuffered R = 10 microemulsions matched very closely that for tributyrin hydrolysis by Lipolase in an aqueous emulsion assay. Apparent activation energies were measured as 13 +/- 2 and 15 +/- 2 kJ mol / respectively...
November 5, 1995: Biotechnology and Bioengineering
G E Crooks, G D Rees, B H Robinson, M Svensson, G R Stephenson
Lipolase and Lipozyme are produced in large quantities (as a result of genetic engineering and overexpression) for the detergents market and provide a cheap source of highly active biocatalysts. Humicola lanuginosa lipase (HIL) and Rhizomucor miehei lipase (RmL) have been isolated in partially purified form from commercial preparations of Lipolase and Lipozyme, respectively. These lipases were solubilized in Aerosol-OT (AOT)-stabilized water-in-oil (w/o) microemulsions in n-heptane. HIL and RmL activity in these microemulsions was assayed by spectrophotometric measurement of the initial rate of p-nitophenyl butyrate hydrolysis, and by chromatographic determination of the initial rate of octyl decanoate synthesis from 1-octanol and decanoic acid...
October 5, 1995: Biotechnology and Bioengineering
Arne Staby, Randi Holm Jensen, Matthias Bensch, Jürgen Hubbuch, Dorte L Dünweber, Janus Krarup, Jacob Nielsen, Mette Lund, Steffen Kidal, Thomas Budde Hansen, Inge Holm Jensen
A comparative study on weak anion exchangers was performed to investigate the pH dependence, binding strength, particle size distribution, and static and dynamic capacity of the chromatographic resins. The resins tested included: DEAE Sepharose FF, Poros 50 D, Fractogel EMD DEAE (M), MacroPrep DEAE Support, DEAE Ceramic HyperD 20, and Toyopearl DEAE 650 M. Testing was performed with five different model proteins: Anti-FVII mAb (immunoglobulin G), aprotinin, bovine serum albumin (BSA), Lipolase (Novozymes), and myoglobin...
September 14, 2007: Journal of Chromatography. A
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