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Lipases and Lipases Modification

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (20 August 2017) | Viewed by 105213

Special Issue Editor

Centre for Chemistry and Biotechnology, School of Life and Environmental Sciences, Faculty of Science, Engineering and Built Environment, Deakin University, 75 Pigdons Road, Geelong, VIC 3216, Australia
Interests: marine bioactives; lipases; omega-3; nanomaterials; graphene; biotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Lipases are important catalysts that are able to function in both aqueous and solvent environments, making them particularly versatile for industrial applications such as the production of fine chemicals, biodiesel production and the formation of new food ingredients. Lipases are able to produce chiral products and can be reused multiple times if immobilised, making them cost effective. In this special issue, we aim to showcase the versatility of lipases as biocatalysts and encourage the submission of manuscripts that describe new uses of lipases, or technology that improves the utility of or mechanistic understanding of lipases as biocatalysts.

Prof. Colin Barrow
Guest Editor

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Keywords

  • lipase
  • immobilisation
  • biocatalyst
  • biodiesel
  • fine chemicals
  • food ingredient
  • kinetic resolution
  • detergents

Published Papers (21 papers)

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24 pages, 3796 KiB  
Article
Kinetics and Optimization of Lipophilic Kojic Acid Derivative Synthesis in Polar Aprotic Solvent Using Lipozyme RMIM and Its Rheological Study
by Nurazwa Ishak, Ahmad Firdaus B. Lajis, Rosfarizan Mohamad, Arbakariya B. Ariff, Mohd Shamzi Mohamed, Murni Halim and Helmi Wasoh
Molecules 2018, 23(2), 501; https://doi.org/10.3390/molecules23020501 - 24 Feb 2018
Cited by 16 | Viewed by 5438
Abstract
The synthesis of kojic acid derivative (KAD) from kojic and palmitic acid (C16:0) in the presence of immobilized lipase from Rhizomucor miehei (commercially known as Lipozyme RMIM), was studied using a shake flask system. Kojic acid is a polyfunctional heterocycles that acts as [...] Read more.
The synthesis of kojic acid derivative (KAD) from kojic and palmitic acid (C16:0) in the presence of immobilized lipase from Rhizomucor miehei (commercially known as Lipozyme RMIM), was studied using a shake flask system. Kojic acid is a polyfunctional heterocycles that acts as a source of nucleophile in this reaction allowing the formation of a lipophilic KAD. In this study, the source of biocatalyst, Lipozyme RMIM, was derived from the lipase of Rhizomucor miehei immobilized on weak anion exchange macro-porous Duolite ES 562 by the adsorption technique. The effects of solvents, enzyme loading, reaction temperature, and substrate molar ratio on the reaction rate were investigated. In one-factor-at-a-time (OFAT) experiments, a high reaction rate (30.6 × 10−3 M·min−1) of KAD synthesis was recorded using acetone, enzyme loading of 1.25% (w/v), reaction time of 12 h, temperature of 50 °C and substrate molar ratio of 5:1. Thereafter, a yield of KAD synthesis was optimized via the response surface methodology (RSM) whereby the optimized molar ratio (fatty acid: kojic acid), enzyme loading, reaction temperature and reaction time were 6.74, 1.97% (w/v), 45.9 °C, and 20 h respectively, giving a high yield of KAD (64.47%). This condition was reevaluated in a 0.5 L stirred tank reactor (STR) where the agitation effects of two impellers; Rushton turbine (RT) and pitch-blade turbine (PBT), were investigated. In the STR, a very high yield of KAD synthesis (84.12%) was achieved using RT at 250 rpm, which was higher than the shake flask, thus indicating better mixing quality in STR. In a rheological study, a pseudoplastic behavior of KAD mixture was proposed for potential application in lotion formulation. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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14 pages, 4699 KiB  
Article
Enhancing the Bioconversion of Azelaic Acid to Its Derivatives by Response Surface Methodology
by Nurshafira Khairudin, Mahiran Basri, Hamid Reza Fard Masoumi, Shazwani Samson and Siti Efliza Ashari
Molecules 2018, 23(2), 397; https://doi.org/10.3390/molecules23020397 - 13 Feb 2018
Cited by 17 | Viewed by 5921
Abstract
Azelaic acid (AzA) and its derivatives have been known to be effective in the treatment of acne and various cutaneous hyperpigmentary disorders. The esterification of azelaic acid with lauryl alcohol (LA) to produce dilaurylazelate using immobilized lipase B from Candida antarctica (Novozym 435) [...] Read more.
Azelaic acid (AzA) and its derivatives have been known to be effective in the treatment of acne and various cutaneous hyperpigmentary disorders. The esterification of azelaic acid with lauryl alcohol (LA) to produce dilaurylazelate using immobilized lipase B from Candida antarctica (Novozym 435) is reported. Response surface methodology was selected to optimize the reaction conditions. A well-fitting quadratic polynomial regression model for the acid conversion was established with regards to several parameters, including reaction time and temperature, enzyme amount, and substrate molar ratios. The regression equation obtained by the central composite design of RSM predicted that the optimal reaction conditions included a reaction time of 360 min, 0.14 g of enzyme, a reaction temperature of 46 °C, and a molar ratio of substrates of 1:4.1. The results from the model were in good agreement with the experimental data and were within the experimental range (R2 of 0.9732).The inhibition zone can be seen at dilaurylazelate ester with diameter 9.0±0.1 mm activities against Staphylococcus epidermidis S273. The normal fibroblasts cell line (3T3) was used to assess the cytotoxicity activity of AzA and AzA derivative, which is dilaurylazelate ester. The comparison of the IC50 (50% inhibition of cell viability) value for AzA and AzA derivative was demonstrated. The IC50 value for AzA was 85.28 μg/mL, whereas the IC50 value for AzA derivative was more than 100 μg/mL. The 3T3 cell was still able to survive without any sign of toxicity from the AzA derivative; thus, it was proven to be non-toxic in this MTT assay when compared with AzA. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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15 pages, 2966 KiB  
Article
Lipase-Produced Hydroxytyrosyl Eicosapentaenoate is an Excellent Antioxidant for the Stabilization of Omega-3 Bulk Oils, Emulsions and Microcapsules
by Taiwo Olusesan Akanbi and Colin James Barrow
Molecules 2018, 23(2), 275; https://doi.org/10.3390/molecules23020275 - 29 Jan 2018
Cited by 33 | Viewed by 4306
Abstract
In this study, several lipophilic hydroxytyrosyl esters were prepared enzymatically using immobilized lipase from Candida antarctica B. Oxidation tests showed that these conjugates are excellent antioxidants in lipid-based matrices, with hydroxytyrosyl eicosapentaenoate showing the highest antioxidant activity. Hydroxytyrosyl eicosapentaenoate effectively stabilized bulk fish [...] Read more.
In this study, several lipophilic hydroxytyrosyl esters were prepared enzymatically using immobilized lipase from Candida antarctica B. Oxidation tests showed that these conjugates are excellent antioxidants in lipid-based matrices, with hydroxytyrosyl eicosapentaenoate showing the highest antioxidant activity. Hydroxytyrosyl eicosapentaenoate effectively stabilized bulk fish oil, fish-oil-in-water emulsions and microencapsulated fish oil. The stabilizing effect of this antioxidant may either be because it orients itself with the omega-3 fatty acids in the oil, thereby protecting them against oxidation, or because this unstable fatty acid can preferentially oxidise, thus providing an additional mechanism of antioxidant protection. Hydroxytyrosyl eicosapentaenoate itself was stable for one year when stored at −20 °C. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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1046 KiB  
Article
One-Pot Lipase-Catalyzed Enantioselective Synthesis of (R)-(−)-N-Benzyl-3-(benzylamino)butanamide: The Effect of Solvent Polarity on Enantioselectivity
by Marina A. Ortega-Rojas, José Domingo Rivera-Ramírez, C. Gabriela Ávila-Ortiz, Eusebio Juaristi, Fernando González-Muñoz, Edmundo Castillo and Jaime Escalante
Molecules 2017, 22(12), 2189; https://doi.org/10.3390/molecules22122189 - 09 Dec 2017
Cited by 11 | Viewed by 3811
Abstract
The use of the solvent engineering has been applied for controlling the resolution of lipase-catalyzed synthesis of β-aminoacids via Michael addition reactions. The strategy consisted of the thermodynamic control of products at equilibrium using the lipase CalB as a catalyst. The enzymatic chemo- [...] Read more.
The use of the solvent engineering has been applied for controlling the resolution of lipase-catalyzed synthesis of β-aminoacids via Michael addition reactions. The strategy consisted of the thermodynamic control of products at equilibrium using the lipase CalB as a catalyst. The enzymatic chemo- and enantioselective synthesis of (R)-(−)-N-benzyl-3-(benzylamino)butanamide is reported, showing the influence of the solvent on the chemoselectivity of the aza-Michael addition and the subsequent kinetic resolution of the Michael adduct; both processes are catalyzed by CalB and both are influenced by the nature of the solvent medium. This approach allowed us to propose a novel one-pot strategy for the enzymatic synthesis of enantiomerically enriched β-aminoesters and β-aminoacids. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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4796 KiB  
Article
One-Step Partially Purified Lipases (ScLipA and ScLipB) from Schizophyllum commune UTARA1 Obtained via Solid State Fermentation and Their Applications
by Yew Chee Kam, Kwan Kit Woo and Lisa Gaik Ai Ong
Molecules 2017, 22(12), 2106; https://doi.org/10.3390/molecules22122106 - 08 Dec 2017
Cited by 3 | Viewed by 4192
Abstract
Lipases with unique characteristics are of value in industrial applications, especially those targeting cost-effectiveness and less downstream processes. The aims of this research were to: (i) optimize the fermentation parameters via solid state fermentation (SSF); and (ii) study the performance in hydrolysis and [...] Read more.
Lipases with unique characteristics are of value in industrial applications, especially those targeting cost-effectiveness and less downstream processes. The aims of this research were to: (i) optimize the fermentation parameters via solid state fermentation (SSF); and (ii) study the performance in hydrolysis and esterification processes of the one-step partially purified Schizophyllum commune UTARA1 lipases. Lipase was produced by cultivating S. commune UTARA1 on sugarcane bagasse (SB) with used cooking oil (UCO) via SSF and its production was optimized using Design-Expert® 7.0.0. Fractions 30% (ScLipA) and 70% (ScLipB) which contained high lipase activity were obtained by stepwise (NH4)2SO4 precipitation. Crude fish oil, coconut oil and butter were used to investigate the lipase hydrolysis capabilities by a free glycerol assay. Results showed that ScLipA has affinities for long, medium and short chain triglycerides, as all the oils investigated were degraded, whereas ScLipB has affinities for long chain triglycerides as it only degrades crude fish oil. During esterification, ScLipA was able to synthesize trilaurin and triacetin. Conversely, ScLipB was specific towards the formation of 2-mono-olein and triacetin. From the results obtained, it was determined that ScLipA and ScLipB are sn-2 regioselective lipases. Hence, the one-step partial purification strategy proved to be feasible for partial purification of S. commune UTARA1 lipases that has potential use in industrial applications. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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5807 KiB  
Article
Improved Performance of Magnetic Cross-Linked Lipase Aggregates by Interfacial Activation: A Robust and Magnetically Recyclable Biocatalyst for Transesterification of Jatropha Oil
by Weiwei Zhang, Huixia Yang, Wanyi Liu, Na Wang and Xiaoqi Yu
Molecules 2017, 22(12), 2157; https://doi.org/10.3390/molecules22122157 - 07 Dec 2017
Cited by 23 | Viewed by 5148
Abstract
Lipases are the most widely employed enzymes in commercial industries. The catalytic mechanism of most lipases involves a step called “interfacial activation”. As interfacial activation can lead to a significant increase in catalytic activity, it is of profound importance in developing lipase immobilization [...] Read more.
Lipases are the most widely employed enzymes in commercial industries. The catalytic mechanism of most lipases involves a step called “interfacial activation”. As interfacial activation can lead to a significant increase in catalytic activity, it is of profound importance in developing lipase immobilization methods. To obtain a potential biocatalyst for industrial biodiesel production, an effective strategy for enhancement of catalytic activity and stability of immobilized lipase was developed. This was performed through the combination of interfacial activation with hybrid magnetic cross-linked lipase aggregates. This biocatalyst was investigated for the immobilization of lipase from Rhizomucor miehei (RML). Under the optimal conditions, the activity recovery of the surfactant-activated magnetic RML cross-linked enzyme aggregates (CLEAs) was as high as 2058%, with a 20-fold improvement over the free RML. Moreover, the immobilized RML showed excellent catalytic performance for the biodiesel reaction at a yield of 93%, and more importantly, could be easily separated from the reaction mixture by simple magnetic decantation, and retained more than 84% of its initial activities after five instances of reuse. This study provides a new and versatile approach for designing and fabricating immobilized lipase with high activation and stability. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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3194 KiB  
Article
Frozen Microemulsions for MAPLE Immobilization of Lipase
by Valeria Califano, Francesco Bloisi, Giuseppe Perretta, Antonio Aronne, Giovanni Ausanio, Aniello Costantini and Luciano Vicari
Molecules 2017, 22(12), 2153; https://doi.org/10.3390/molecules22122153 - 05 Dec 2017
Cited by 16 | Viewed by 3644
Abstract
Candida rugosa lipase (CRL) was deposited by matrix assisted pulsed laser evaporation (MAPLE) in order to immobilize the enzyme with a preserved native conformation, which ensures its catalytic functionality. For this purpose, the composition of the MAPLE target was optimized by adding the [...] Read more.
Candida rugosa lipase (CRL) was deposited by matrix assisted pulsed laser evaporation (MAPLE) in order to immobilize the enzyme with a preserved native conformation, which ensures its catalytic functionality. For this purpose, the composition of the MAPLE target was optimized by adding the oil phase pentane to a water solution of the amino acid 3-(3,4-dihydroxyphenyl)-2-methyl-l-alanine (m-DOPA), giving a target formed by a frozen water-lipase-pentane microemulsion. Fourier transform infrared (FTIR) spectroscopy and atomic force microscopy (AFM) were used to investigate the structure of MAPLE deposited lipase films. FTIR deconvolution of amide I band indicated a reduction of unfolding and aggregation, i.e., a better preserved lipase secondary structure in the sample deposited from the frozen microemulsion target. AFM images highlighted the absence of big aggregates on the surface of the sample. The functionality of the immobilized enzyme to promote transesterification was determined by thin layer chromatography, resulting in a modified specificity. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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4440 KiB  
Article
Monitoring the Activity of Immobilized Lipase with Quinizarin Diester Fluoro-Chromogenic Probe
by Carolina Aparecida Sabatini, Denis Massucatto dos Santos, Sabrina Matos de Oliveira da Silva and Marcelo Henrique Gehlen
Molecules 2017, 22(12), 2136; https://doi.org/10.3390/molecules22122136 - 04 Dec 2017
Cited by 9 | Viewed by 4270
Abstract
Quinizarin diester is used as a fluoro-chromogenic substrate of the activity of lipase supported in poly(methylmetacrylate) beads (CALB, Novozym® 435) dispersed in organic solvents. The monoester and diester of quinizarin are both non-fluorescent species contrasting with the enzymatic product quinizarin that shows [...] Read more.
Quinizarin diester is used as a fluoro-chromogenic substrate of the activity of lipase supported in poly(methylmetacrylate) beads (CALB, Novozym® 435) dispersed in organic solvents. The monoester and diester of quinizarin are both non-fluorescent species contrasting with the enzymatic product quinizarin that shows optical absorption in the visible region and strong fluorescence signal. The enzymatic conversion is accomplished by spectroscopic measurements and it follows a sigmoid curve from which the mean reaction time of the enzymatic process can be determined. This parameter indicates the enzyme activity of the immobilized lipase. Its dependency with the amount of lipase allowed the determination of the ratio of the catalytic rate and the Michaelis constant (kc/Km) and the experimental value found was (1.0 ± 0.1) × 10−2 mg−1/min in the case of quinizarin diacetate. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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4699 KiB  
Article
Preparation and Characterization of Cellulose Triacetate as Support for Lecitase Ultra Immobilization
by Francielle Batista da Silva, Wilson Galvão de Morais Júnior, Cleuzilene Vieira da Silva, Andressa Tironi Vieira, Antônio Carlos Ferreira Batista, Anízio Márcio de Faria and Rosana Maria Nascimento Assunção
Molecules 2017, 22(11), 1930; https://doi.org/10.3390/molecules22111930 - 16 Nov 2017
Cited by 15 | Viewed by 6061
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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2786 KiB  
Article
An Efficient Approach for Lipase-Catalyzed Synthesis of Retinyl Laurate Nutraceutical by Combining Ultrasound Assistance and Artificial Neural Network Optimization
by Shang-Ming Huang, Hsin-Ju Li, Yung-Chuan Liu, Chia-Hung Kuo and Chwen-Jen Shieh
Molecules 2017, 22(11), 1972; https://doi.org/10.3390/molecules22111972 - 15 Nov 2017
Cited by 15 | Viewed by 3364
Abstract
Although retinol is an important nutrient, retinol is highly sensitive to oxidation. At present, some ester forms of retinol are generally used in nutritional supplements because of its stability and bioavailability. However, such esters are commonly synthesized by chemical procedures which are harmful [...] Read more.
Although retinol is an important nutrient, retinol is highly sensitive to oxidation. At present, some ester forms of retinol are generally used in nutritional supplements because of its stability and bioavailability. However, such esters are commonly synthesized by chemical procedures which are harmful to the environment. Thus, this study utilized a green method using lipase as a catalyst with sonication assistance to produce a retinol derivative named retinyl laurate. Moreover, the process was optimized by an artificial neural network (ANN). First, a three-level-four-factor central composite design (CCD) was employed to design 27 experiments, which the highest relative conversion was 82.64%. Further, the optimal architecture of the CCD-employing ANN was developed, including the learning Levenberg-Marquardt algorithm, the transfer function (hyperbolic tangent), iterations (10,000), and the nodes of the hidden layer (6). The best performance of the ANN was evaluated by the root mean squared error (RMSE) and the coefficient of determination (R2) from predicting and observed data, which displayed a good data-fitting property. Finally, the process performed with optimal parameters actually obtained a relative conversion of 88.31% without long-term reactions, and the lipase showed great reusability for biosynthesis. Thus, this study utilizes green technology to efficiently produce retinyl laurate, and the bioprocess is well established by ANN-mediated modeling and optimization. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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2950 KiB  
Article
Yarrowia lipolytica Extracellular Lipase Lip2 as Biocatalyst for the Ring-Opening Polymerization of ε-Caprolactone
by Karla A. Barrera-Rivera and Antonio Martínez-Richa
Molecules 2017, 22(11), 1917; https://doi.org/10.3390/molecules22111917 - 07 Nov 2017
Cited by 8 | Viewed by 4552
Abstract
Yarrowia lipolytica (YL) is a “non-conventional” yeast that is capable of producing important metabolites. One of the most important products that is secreted by this microorganism is lipase, a ubiquitous enzyme that has considerable industrial potential and can be used as a biocatalyst [...] Read more.
Yarrowia lipolytica (YL) is a “non-conventional” yeast that is capable of producing important metabolites. One of the most important products that is secreted by this microorganism is lipase, a ubiquitous enzyme that has considerable industrial potential and can be used as a biocatalyst in the pharmaceutical, food, and environmental industries. In this work, Yarrowia lipolytica lipase (YLL) was immobilized on Lewatit and Amberlite beads and is used in the enzymatic ring-opening polymerization (ROP) of cyclic esters in the presence of different organic solvents. YLL immobilized on Amberlite XAD7HP had the higher protein adsorption (96%) and a lipolytic activity of 35 U/g. Lewatit VPOC K2629 has the higher lipolytic activity (805 U/g) and 92% of protein adsorption. The highest molecular weight (Mn 10,685 Da) was achieved at 90 °C using YLL that was immobilized on Lewatit 1026 with decane as solvent after 60 h and 100% of monomer conversion. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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980 KiB  
Article
Lipase-Catalyzed Transesterification of Egg-Yolk Phophatidylcholine with Concentrate of n-3 Polyunsaturated Fatty Acids from Cod Liver Oil
by Anna Chojnacka, Witold Gładkowski and Aleksandra Grudniewska
Molecules 2017, 22(10), 1771; https://doi.org/10.3390/molecules22101771 - 19 Oct 2017
Cited by 19 | Viewed by 5048
Abstract
Phospholipids containing PUFAs are important vehicles for their delivering to the targeted tissues. In our research project we established enzymatic methods for the enrichment of natural egg-yolk PC with n-3 PUFAs. Instead of synthetic PUFA ethyl esters, the new strategy was developed using [...] Read more.
Phospholipids containing PUFAs are important vehicles for their delivering to the targeted tissues. In our research project we established enzymatic methods for the enrichment of natural egg-yolk PC with n-3 PUFAs. Instead of synthetic PUFA ethyl esters, the new strategy was developed using polyunsaturated fatty acids enriched fraction (PUFA-EF) from cod liver oil as the natural acyl donors. PUFA-EF was produced by urea-complexation and contained 86.9% PUFA including 8.5% stearidonic acid (SDA; 18:4(n-3)), 26.7% EPA, and 45.2% DHA. The transesterification of PC with PUFA was catalyzed by lipases. After screening of enzymes the effect of reaction medium; molar ratio of substrates and etc. was investigated. The highest incorporation of PUFA was 45.6%; including 36.8% DHA and 5.8% EPA at the following reaction conditions: hexane; 55 °C; PUFA-EF/PC acyl ratio of 10; 48 h of reaction time and lipase B from Candida antarctica as a biocatalyst (20% of enzyme load). Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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820 KiB  
Article
Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil
by Lívia T. de A. Souza, Sonia Moreno-Perez, Gloria Fernández Lorente, Eliane P. Cipolatti, Débora De Oliveira, Rodrigo R. Resende and Benevides C. Pessela
Molecules 2017, 22(10), 1508; https://doi.org/10.3390/molecules22101508 - 25 Sep 2017
Cited by 17 | Viewed by 3868
Abstract
The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 [...] Read more.
The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25–48 °C) and pH (6.5–8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme–substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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3218 KiB  
Article
Glycyrrhetinic Acid Liposomes Containing Mannose-Diester Lauric Diacid-Cholesterol Conjugate Synthesized by Lipase-Catalytic Acylation for Liver-Specific Delivery
by Jing Chen, Yuchao Chen, Yi Cheng and Youheng Gao
Molecules 2017, 22(10), 1598; https://doi.org/10.3390/molecules22101598 - 24 Sep 2017
Cited by 15 | Viewed by 5239
Abstract
Mannose-diester lauric diacid-cholesterol (Man-DLD-Chol), as a liposomal target ligand, was synthesized by lipase catalyzed in a non-aqueous medium. Its chemical structure was confirmed by mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. Glycyrrhetinic acid (GA) liposomes containing Man-DLD-Chol (Man-DLD-Chol-GA-Lp) were prepared by [...] Read more.
Mannose-diester lauric diacid-cholesterol (Man-DLD-Chol), as a liposomal target ligand, was synthesized by lipase catalyzed in a non-aqueous medium. Its chemical structure was confirmed by mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. Glycyrrhetinic acid (GA) liposomes containing Man-DLD-Chol (Man-DLD-Chol-GA-Lp) were prepared by the film-dispersion method. We evaluated the characterizations of liposomes, drug-release in vitro, the hemolytic test, cellular uptake, pharmacokinetics, and the tissue distributions. The cellular uptake in vitro suggested that the uptake of Man-DLD-Chol-modified liposomes was significantly higher than that of unmodified liposomes in HepG2 cells. Pharmacokinetic parameters indicated that Man-DLD-Chol-GA-Lp was eliminated more rapidly than GA-Lp. In tissue distributions, the targeting efficiency (Te) of Man-DLD-Chol-GA-Lp on liver was 54.67%, relative targeting efficiency (RTe) was 3.39, relative uptake rate (Re) was 4.78, and peak concentration ratio (Ce) was 3.46. All these results supported the hypothesis that Man-DLD-Chol would be an efficient liposomal carrier, and demonstrated that Man-DLD-Chol-GA-Lp has potential as a drug delivery for liver-targeting therapy. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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2935 KiB  
Article
Improving the Efficiency of New Automatic Dishwashing Detergent Formulation by Addition of Thermostable Lipase, Protease and Amylase
by Ashwini Naganthran, Malihe Masomian, Raja Noor Zaliha Raja Abd. Rahman, Mohd Shukuri Mohamad Ali and Hisham Mohd Nooh
Molecules 2017, 22(9), 1577; https://doi.org/10.3390/molecules22091577 - 19 Sep 2017
Cited by 34 | Viewed by 9309
Abstract
The use of T1 lipase in automatic dishwashing detergent (ADD) is well established, but efficiency in hard water is very low. A new enzymatic environmentally-friendly dishwashing was formulated to be efficient in both soft and hard water. Thermostable enzymes such as T1 lipase [...] Read more.
The use of T1 lipase in automatic dishwashing detergent (ADD) is well established, but efficiency in hard water is very low. A new enzymatic environmentally-friendly dishwashing was formulated to be efficient in both soft and hard water. Thermostable enzymes such as T1 lipase from Geobacillus strain T1, Rand protease from Bacillus subtilis strain Rand, and Maltogenic amylase from Geobacillus sp. SK70 were produced and evaluated for an automatic dishwashing detergent formulation. The components of the new ADD were optimized for compatibility with these three enzymes. In compatibility tests of the enzymes with different components, several criteria were considered. The enzymes were mostly stable in non-ionic surfactants, especially polyhydric alcohols, Glucopon UP 600, and in a mixture of sodium carbonate and glycine (30:70) buffer at a pH of 9.25. Sodium polyacrylate and sodium citrate were used in the ADD formulation as a dispersing agent and a builder, respectively. Dishwashing performance of the formulated ADDs was evaluated in terms of percent of soil removed using the Leenert‘s Improved Detergency Tester. The results showed that the combination of different hydrolysis enzymes could improve the washing efficiency of formulated ADD compared to the commercial ADD “Finish” at 40 and 50 C. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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3501 KiB  
Article
Transesterification Synthesis of Chloramphenicol Esters with the Lipase from Bacillus amyloliquefaciens
by Fengying Dong, Lingmeng Li, Lin Lin, Dannong He, Jingwen Chen, Wei Wei and Dongzhi Wei
Molecules 2017, 22(9), 1523; https://doi.org/10.3390/molecules22091523 - 19 Sep 2017
Cited by 11 | Viewed by 5900
Abstract
This work presents a synthetic route to produce chloramphenicol esters by taking advantage the high enantio- and regio-selectivity of lipases. A series of chloramphenicol esters were synthesized using chloramphenicol, acyl donors of different carbon chain length and lipase LipBA (lipase cloned from [...] Read more.
This work presents a synthetic route to produce chloramphenicol esters by taking advantage the high enantio- and regio-selectivity of lipases. A series of chloramphenicol esters were synthesized using chloramphenicol, acyl donors of different carbon chain length and lipase LipBA (lipase cloned from Bacillus amyloliquefaciens). Among acyl donors with different carbon chain lengths, vinyl propionate was found to be the best. The influences of different organic solvents, reaction temperature, reaction time, enzyme loading and water content on the synthesis of the chloramphenicol esters were studied. The synthesis of chloramphenicol propionate (0.25 M) with 4.0 g L−1 of LipBA loading gave a conversion of ~98% and a purity of ~99% within 8 h at 50 °C in 1,4-dioxane as solvent. The optimum mole ratio of vinyl propionate to chloramphenicol was increased to 5:1. This is the first report of B. amyloliquefaciens lipase being used in chloramphenicol ester synthesis and a detailed study of the synthesis of chloramphenicol propionate using this reaction. The high enzyme activity and selectivity make lipase LipBA an attractive catalyst for green chemical synthesis of molecules with complex structures. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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1374 KiB  
Article
Statistical Methodologies for the Optimization of Lipase and Biosurfactant by Ochrobactrum intermedium Strain MZV101 in an Identical Medium for Detergent Applications
by Gholamhossein Ebrahimipour, Hossein Sadeghi and Mina Zarinviarsagh
Molecules 2017, 22(9), 1460; https://doi.org/10.3390/molecules22091460 - 11 Sep 2017
Cited by 13 | Viewed by 4302
Abstract
The Plackett–Burman design and the Box–Behnken design, statistical methodologies, were employed for the optimization lipase and biosurfactant production by Ochrobactrum intermedium strain MZV101 in an identical broth medium for detergent applications. Environmental factor pH determined to be most mutual significant variables on production. [...] Read more.
The Plackett–Burman design and the Box–Behnken design, statistical methodologies, were employed for the optimization lipase and biosurfactant production by Ochrobactrum intermedium strain MZV101 in an identical broth medium for detergent applications. Environmental factor pH determined to be most mutual significant variables on production. A high concentration of molasses at high temperature and pH has a negative effect on lipase and biosurfactant production by O. intermedium strain MZV101. The chosen mathematical method of medium optimization was sufficient for improving the industrial production of lipase and biosurfactant by bacteria, which were respectively increased 3.46- and 1.89-fold. The duration of maximum production became 24 h shorter, so it was fast and cost-saving. In conclusion, lipase and biosurfactant production by O. intermedium strain MZV101 in an identical culture medium at pH 10.5–11 and 50–60 °C, with 1 g/L of molasses, seemed to be economical, fast, and effective for the enhancement of yield percentage for use in detergent applications. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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1525 KiB  
Article
Different Covalent Immobilizations Modulate Lipase Activities of Hypocrea pseudokoningii
by Marita G. Pereira, Susana Velasco-Lozano, Sonia Moreno-Perez, Aline M. Polizeli, Paulo R. Heinen, Fernanda D. A. Facchini, Ana C. Vici, Mariana Cereia, Benevides C. Pessela, Gloria Fernandez-Lorente, Jose M. Guisan, João A. Jorge and Maria De Lourdes T. M. Polizeli
Molecules 2017, 22(9), 1448; https://doi.org/10.3390/molecules22091448 - 04 Sep 2017
Cited by 6 | Viewed by 4213
Abstract
Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four chemical supports: agarose activated with cyanogen bromide (CNBr), glyoxyl-agarose (GX), MANAE-agarose activated with glutaraldehyde (GA) and GA-crosslinked with glutaraldehyde. Results [...] Read more.
Enzyme immobilization can promote several advantages for their industrial application. In this work, a lipase from Hypocrea pseudokoningii was efficiently linked to four chemical supports: agarose activated with cyanogen bromide (CNBr), glyoxyl-agarose (GX), MANAE-agarose activated with glutaraldehyde (GA) and GA-crosslinked with glutaraldehyde. Results showed a more stable lipase with both the GA-crosslinked and GA derivatives, compared to the control (CNBr), at 50 °C, 60 °C and 70 °C. Moreover, all derivatives were stabilized when incubated with organic solvents at 50%, such as ethanol, methanol, n-propanol and cyclohexane. Furthermore, lipase was highly activated (4-fold) in the presence of cyclohexane. GA-crosslinked and GA derivatives were more stable than the CNBr one in the presence of organic solvents. All derivatives were able to hydrolyze sardine, açaí (Euterpe oleracea), cotton seed and grape seed oils. However, during the hydrolysis of sardine oil, GX derivative showed to be 2.3-fold more selectivity (eicosapentaenoic acid (EPA)/docosahexaenoic acid (DHA) ratio) than the control. Additionally, the types of immobilization interfered with the lipase enantiomeric preference. Unlike the control, the other three derivatives preferably hydrolyzed the R-isomer of 2-hydroxy-4-phenylbutanoic acid ethyl ester and the S-isomer of 1-phenylethanol acetate racemic mixtures. On the other hand, GX and CNBr derivatives preferably hydrolyzed the S-isomer of butyryl-2-phenylacetic acid racemic mixture while the GA and GA-crosslink derivatives preferably hydrolyzed the R-isomer. However, all derivatives, including the control, preferably hydrolyzed the methyl mandelate S-isomer. Moreover, the derivatives could be used for eight consecutive cycles retaining more than 50% of their residual activity. This work shows the importance of immobilization as a tool to increase the lipase stability to temperature and organic solvents, thus enabling the possibility of their application at large scale processes. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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3476 KiB  
Article
The Role of Solvent-Accessible Leu-208 of Cold-Active Pseudomonas fluorescens Strain AMS8 Lipase in Interfacial Activation, Substrate Accessibility and Low-Molecular Weight Esterification in the Presence of Toluene
by Norhayati Yaacob, Nor Hafizah Ahmad Kamarudin, Adam Thean Chor Leow, Abu Bakar Salleh, Raja Noor Zaliha Raja Abd Rahman and Mohd Shukuri Mohamad Ali
Molecules 2017, 22(8), 1312; https://doi.org/10.3390/molecules22081312 - 12 Aug 2017
Cited by 27 | Viewed by 4810
Abstract
The alkaline cold-active lipase from Pseudomonas fluorescens AMS8 undergoes major structural changes when reacted with hydrophobic organic solvents. In toluene, the AMS8 lipase catalytic region is exposed by the moving hydrophobic lid 2 (Glu-148 to Gly-167). Solvent-accessible surface area analysis revealed that Leu-208, [...] Read more.
The alkaline cold-active lipase from Pseudomonas fluorescens AMS8 undergoes major structural changes when reacted with hydrophobic organic solvents. In toluene, the AMS8 lipase catalytic region is exposed by the moving hydrophobic lid 2 (Glu-148 to Gly-167). Solvent-accessible surface area analysis revealed that Leu-208, which is located next to the nucleophilic Ser-207 has a focal function in influencing substrate accessibility and flexibility of the catalytic pocket. Based on molecular dynamic simulations, it was found that Leu-208 strongly facilitates the lid 2 opening via its side-chain. The KM and Kcat/KM of L208A mutant were substrate dependent as it preferred a smaller-chain ester (pNP-caprylate) as compared to medium (pNP-laurate) or long-chain (pNP-palmitate) esters. In esterification of ethyl hexanoate, L208A promotes a higher ester conversion rate at 20 °C but not at 30 °C, as a 27% decline was observed. Interestingly, the wild-type (WT) lipase’s conversion rate was found to increase with a higher temperature. WT lipase AMS8 esterification was higher in toluene as compared to L208A. Hence, the results showed that Leu-208 of AMS8 lipase plays an important role in steering a broad range of substrates into its active site region by regulating the flexibility of this region. Leu-208 is therefore predicted to be crucial for its role in interfacial activation and catalysis in toluene. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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6534 KiB  
Article
Preparation of Carriers Based on ZnO Nanoparticles Decorated on Graphene Oxide (GO) Nanosheets for Efficient Immobilization of Lipase from Candida rugosa
by Shan Zhang, Jie Shi, Qianchun Deng, Mingming Zheng, Chuyun Wan, Chang Zheng, Ya Li and Fenghong Huang
Molecules 2017, 22(7), 1205; https://doi.org/10.3390/molecules22071205 - 19 Jul 2017
Cited by 28 | Viewed by 5365
Abstract
Herein, a promising carrier, graphene oxide (GO) decorated with ZnO nanoparticles, denoted as GO/ZnO composite, has been designed and constructed. This carrier was characterized by X-ray powder diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetry. Then, Candida rugosa lipase (CRL) was [...] Read more.
Herein, a promising carrier, graphene oxide (GO) decorated with ZnO nanoparticles, denoted as GO/ZnO composite, has been designed and constructed. This carrier was characterized by X-ray powder diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetry. Then, Candida rugosa lipase (CRL) was immobilized onto the GO-based materials via physical adsorption. Our results indicated that the lipase loading amount on the GO/ZnO composites was about 73.52 mg of protein per g. In the activity assay, the novel immobilized lipase GO/ZnO@CRL, exhibited particularly excellent performance in terms of thermostability and reusability. Within 30 min at 50 °C, the free lipase, GO@CRL and ZnO@CRL had respectively lost 64%, 62% and 41% of their initial activity. However, GO/ZnO@CRL still retained its activity of 63% after 180 min at 50 °C. After reuse of the GO/ZnO@CRL 14 times, 90% of the initial activity can be recovered. Meanwhile, the relative activity of GO@CRL and ZnO@CRL was 28% and 23% under uniform conditions. Hence, GO-decorated ZnO nanoparticles may possess great potential as carriers for immobilizing lipase in a wide range of applications. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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Review

Jump to: Research

875 KiB  
Review
Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression
by Daniel Prieto and Pablo Oppezzo
Molecules 2017, 22(12), 2083; https://doi.org/10.3390/molecules22122083 - 05 Dec 2017
Cited by 12 | Viewed by 5583
Abstract
Lipoprotein lipase (LPL) is a central enzyme in lipid metabolism. Due to its catalytic activity, LPL is involved in metabolic pathways exploited by various solid and hematologic malignancies to provide an extra energy source to the tumor cell. We and others described a [...] Read more.
Lipoprotein lipase (LPL) is a central enzyme in lipid metabolism. Due to its catalytic activity, LPL is involved in metabolic pathways exploited by various solid and hematologic malignancies to provide an extra energy source to the tumor cell. We and others described a link between the expression of LPL in the tumor cell and a poor clinical outcome of patients suffering Chronic Lymphocytic Leukemia (CLL). This leukemia is characterized by a slow accumulation of mainly quiescent clonal CD5 positive B cells that infiltrates secondary lymphoid organs, bone marrow and peripheral blood. Despite LPL being found to be a reliable molecular marker for CLL prognosis, its functional role and the molecular mechanisms regulating its expression are still matter of debate. Herein we address some of these questions reviewing the current state of the art of LPL research in CLL and providing some insights into where currently unexplored questions may lead to. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification)
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