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Lipases and Phospholipases in Biocatalysis

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A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 47630

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Prof. Dr. Witold Gładkowski

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Department of Chemistry, Wrocław University of Environmental and Life Science, Wrocław, Poland
Interests: biotransformations of organic compounds by whole cells; chemoenzymatic synthesis of optically active lactones with biological activity; determination of absolute configurations of optically active compounds; enzymatic modifications of phospholipids; analytical and spectroscopic methods to establish the structure of new compounds
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Dear Colleagues,

Lipases and phospholipases are ubiquitous enzymes in most living organisms, including animals, plants, yeasts, fungi, and bacteria. After proteases and carbohydrases, lipases represent the third most commercialized enzymes, constituting more than one-fifth of the global enzyme market. These environmentally friendly enzymes catalyze hydrolysis of ester bonds of triacylglycerols and phospholipids, respectively. In addition to the activity of hydrolases, they also catalyze esterification, transesterification, and interesterification reactions, and phospholipases also show acyltransferase, transacylase, and transphosphatidylation activities. Moreover, these biocatalysts have broad substrate specificity, high enantioselectivity, as well as stability in organic solvents and at extreme temperatures and pH. Thus, lipases and phospholipases represent a versatile group of biocatalysts that are widely used in asymmetric synthesis to produce optically active compounds or their precursors by the kinetic or dynamic kinetic resolution of racemates. Another usage of their catalytic activity is the modification of lipids to produce molecules with different physical and/or nutritional properties. Thus, lipases and phospholipases have found application in fine chemistry, pharmacy, agriculture, the food industry, and cosmetics.

Today, native enzymes of different origin are used for biocatalytic processes after isolation and purification. To improve their stability and catalytic properties, different strategies are used, namely, their immobilization by different techniques, or development of molecular techniques for the production of recombinant heterologous proteins in a host system allowing high-level protein expression and production of new redesigned enzymes.

For this Special Issue, contributions from new aspects of application of lipases and phospholipases in biocatalysis are welcomed, both in laboratory and industrial scale, including resolution of racemic mixtures and modification of lipids.

DSc. Witold Gładkowski
Guest Editor

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Keywords

Kinetic/dynamic resolution of racemates catalyzed by lipases/phospholipases
Modification of lipids catalyzed by lipases/phospholipases
Isolation and biocatalytic properties of native lipases/phospholipases from new sources
New application of commercially available free and immobilized lipases/phosholipases to produce chemicals, pharmaceuticals, nutraceuticals, etc.
Immobilization of lipases/phospholipases and their application in biocatalysis
Protein engineering strategies for the improvement of catalytic and stability properties of lipases/phospholipases.

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Published Papers (9 papers)

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Research

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20 pages, 3897 KiB

Open AccessArticle

Heterologous Expression and Characterization of Plant Lipase LIP2 from Elaeis guineensis Jacq. Oil Palm Mesocarp in Escherichia coli

by Mohd Hadzdee Mohd Din, Anusha Nair, Malihe Masomian, Mohd Shukuri Mohamad Ali and Raja Noor Zaliha Raja Abd. Rahman

Catalysts 2021, 11(2), 244; https://doi.org/10.3390/catal11020244 - 12 Feb 2021

Cited by 4 | Viewed by 2707

Abstract

In order to determine the potential of biochemical and structural features of Elaeis guineensis Jacq. oil palm mesocarp lipases, the LIP2 gene was isolated, expressed, purified and characterized through the Escherichia coli microbial recombinant system. Gene analysis of LIP2 revealed that it is composed of 1584 base pairs which are encoded in 528 amino acid residues with a molecular weight of around 57 kDa. LIP2 has distinctive lipolytic properties in terms of α/β fold and the catalytic triad for lipase. The LIP2 lipase was successfully expressed and purified from E. coli Rosetta (DE3) via affinity chromatography. The optimal temperature and pH for the lipase activity was 30 °C and a pH of 9, respectively. Stability was profoundly increased with the addition of metal ions (Ca²⁺, Mg²⁺, Mn⁺, and Ni⁺), along with organic solvents (ethanol and octanol). pNP myristate was the most suitable among all pNP esters. In biophysical characterization analysis, LIP2 has a thermal denaturing point at 66 °C, which mostly consists of random patterns (39.8%) followed by α-helix (30.3%), turns (23.8%) and β-sheet (6.2%). From the successful purification and characterization, the potential of oil palm mesocarp lipase was able to be further explored. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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15 pages, 2316 KiB

Open AccessFeature PaperArticle

Comparative Studies on the Susceptibility of (R)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases

by Paweł Mituła, Czesław Wawrzeńczyk and Witold Gładkowski

Catalysts 2021, 11(1), 129; https://doi.org/10.3390/catal11010129 - 16 Jan 2021

Cited by 1 | Viewed by 1921

Abstract

Susceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and its phosphono analogue (R)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substrates at sn-1 position was carried out by lipase from Mucor miehei (Lipozyme^®) and lipase B from Candida antarctica (Novozym 435) in 95% ethanol at 30 °C, and the hydrolysis with Lecitase^TM Ultra was carried out in hexane/water at 50 °C. Hydrolysis at sn-2 position was carried out in isooctane/Tris-HCl/AOT system at 40 °C using phospholipase A₂ (PLA₂) from porcine pancreas and PLA₂ from bovine pancreas or 25 °C using PLA₂ from bee venom. Hydrolysis in the polar part of the studied compounds was carried out at 30 °C in acetate buffer/ethyl acetate system using phospholipase D (PLD) from Streptococcus sp. and PLD from white cabbage or in Tris-HCl buffer/methylene chloride system at 35 °C using PLD from Streptomyces chromofuscus. The results showed that the presence of C-P bond between glycerol and phosphoric acid residue in DPPnC increases the rate of enzymatic hydrolysis or ethanolysis of ester bonds at the sn-1 and sn-2 position and decreases the rate of hydrolysis in the polar head of the molecule. The most significant changes in the reaction rates were observed for reaction with PLD from Streptococcus sp. and PLD from Streptomyces chromofuscus that hydrolyzed DPPnC approximately two times slower than DPPC and soybean PC. The lower susceptibility of DPPnC towards enzymatic hydrolysis by phospholipases D gives hope for the possibility of using DPPnC-like phosphonolipids as the carriers of bioactive molecules that, instead of choline, can be bounded with diacylpropylphosphonic acids (DPPnA). Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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16 pages, 1978 KiB

Open AccessArticle

Valorization of Corn Seed Oil Acid Degumming Waste for Phospholipids Preparation by Phospholipase D-Mediated Processes

by Chiara Allegretti, Andrea Bono, Paola D’Arrigo, Francesca Denuccio, Davide De Simeis, Giuseppe Di Lecce, Stefano Serra, Davide Tessaro and Mariacristina Viola

Catalysts 2020, 10(7), 809; https://doi.org/10.3390/catal10070809 - 21 Jul 2020

Cited by 6 | Viewed by 3915

Abstract

This work focused on the phospholipase D-mediated treatment of the waste residue coming from acid degumming, which constitutes the second part of the degumming step in the crude corn edible oil refining process. This industrial process produces a complex by-product (called gum), a mixture containing phospholipids (PLs) whose composition depends on the nature of the oil source. This residue is usually disposed of with the consequential costs and environmental concerns. An efficient multistep protocol of physical separations of the PL-rich fraction from waste gums has been set up, including centrifugation, precipitation and solvent partitioning. This waste stream, which is thoroughly characterized after the concentration process, constitutes a renewable feedstock for the production of value-added PLs with modified polar head-exploiting phospholipase D-mediated biotransformations, which have been successfully performed on this complex natural mixture. The valorization of these waste gums through the production of high value PLs for targeted applications paves the way to a new alternative approach for their disposal, which could be of great interest from a circular economy perspective. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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17 pages, 2752 KiB

Open AccessFeature PaperArticle

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

by Aleksandra Leśniarek, Anna Chojnacka, Radosław Drozd, Magdalena Szymańska and Witold Gładkowski

Catalysts 2020, 10(7), 798; https://doi.org/10.3390/catal10070798 - 17 Jul 2020

Cited by 2 | Viewed by 2515

Abstract

Lecitase™ Ultra was immobilized on four different supports and tested for the first time as the biocatalyst in the kinetic resolution of racemic allyl alcohols with the (E)-4-arylbut-3-en-2-ol system in the process of transesterification. The most effective biocatalyst turned out to be the enzyme immobilized on agarose activated with cyanogen bromide (LU-CNBr). The best results (E > 200, ee_s and ee_p = 95–99%) were obtained for (E)-4-phenylbut-3-en-2-ol and its analog with a 2,5-dimethylphenyl ring whereas the lowest ee of kinetic resolution products (90%) was achieved for the substrate with a 4-methoxyphenyl substituent. For all substrates, (R)-enantiomers were esterified faster than their (S)-antipodes. The results showed that LU-CNBr is a versatile biocatalyst, showing high activity and enantioselectivity in a wide range of organic solvents in the presence of commonly used acyl donors. High operational stability of LU-CNBr allows it to be reused in three subsequent reaction cycles without negative effects on the efficiency and enantioselectivity of transesterification. This biocatalyst can become attractive to the commercial lipases in the process of the kinetic resolution of allyl alcohols. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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16 pages, 4155 KiB

Open AccessArticle

Synthesis of Lipase-Immobilized CeO₂ Nanorods as Heterogeneous Nano-Biocatalyst for Optimized Biodiesel Production from Eruca sativa Seed Oil

by Anam Fatima, Muhammad Waseem Mumtaz, Hamid Mukhtar, Sadia Akram, Tooba Touqeer, Umer Rashid, Muhammad Raza Ul Mustafa, Imededdine Arbi Nehdi and Mohd Izham Saiman

Catalysts 2020, 10(2), 231; https://doi.org/10.3390/catal10020231 - 15 Feb 2020

Cited by 25 | Viewed by 3412

Abstract

Biodiesel has emerged as one of the most attractive alternative energy sources to meet the growing needs of energy. Many approaches have been adopted for biodiesel synthesis. In the present work, biodiesel was produced from non-edible Eruca sativa oil using nano-biocatalyst-catalysed transesterification. Nano-biocatalyst (CeO₂@PDA@A. terreus Lipase) was developed via the immobilization of lipase on polydopamine coated ceria nanorods, and CeO₂ nanorods were developed via a hydrothermal process. The mean diameter of nanorods were measured to be 50–60 nm, while their mean length was 150–200 nm. Lipase activity before and after immobilization was measured to be 18.32 and 16.90 U/mg/min, respectively. The immobilized lipase depicted high stability at high temperature and pH. CeO₂@PDA@A. terreus Lipase-catalysed transesterification resulted in 89.3% yield of the product. Process optimization through response surface methodology was also executed, and it was depicted that the optimum/maximum E. sativa oil-based biodiesel yield was procured at conditions of 10% CeO₂@PDA@A. terreus Lipase, 6:1 methanol/oil ratio, 0.6% water content, 35 °C reaction temperature, and 30 h reaction time. The fuel compatibility of synthesized biodiesel was confirmed via the estimation of fuel properties that were in agreement with the ASTM D standard. The nanorods and dopamine-modified nanorods were characterized by FTIR spectroscopy, SEM, and energy dispersive X-ray (EDX), while conversion of E. sativa oil to biodiesel was confirmed by GC/MS and FTIR spectroscopy. Conclusively, it was revealed that CeO₂@PDA@A. terreus Lipase has potential to be employed as an emphatic nano-biocatalyst. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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Review

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19 pages, 5336 KiB

Open AccessReview

Polar Head Modified Phospholipids by Phospholipase D-Catalyzed Transformations of Natural Phosphatidylcholine for Targeted Applications: An Overview

by Chiara Allegretti, Francesca Denuccio, Letizia Rossato and Paola D’Arrigo

Catalysts 2020, 10(9), 997; https://doi.org/10.3390/catal10090997 - 1 Sep 2020

Cited by 18 | Viewed by 6693

Abstract

This review describes the use of phospholipase D (PLD) to perform the transphosphatidylation of the most common natural phospholipid (PL), phosphatidylcholine (PC) to obtain polar head modified phospholipids with real targeted applications. The introduction of different polar heads with distinctive physical and chemical properties such as charge, polarity and dimensions allows the obtainment of very different PLs, which can be exploited in very diverse fields of application. Moreover, the inclusions of a bioactive moiety in the PL polar head constitutes a powerful tool for the stabilization and administration of active ingredients. The use of this biocatalytic approach allows the preparation of compounds which cannot be easily obtained by classical chemical methods, by using mild and green reaction conditions. PLD is a very versatile enzyme, able to catalyze both the hydrolysis of PC to choline and phosphatidic acid (PA), and the transphosphatidylation reaction in the presence of an appropriate alcohol. The yield of production of the desired product and the ratio with the collateral PA formation is highly dependent on parameters such as the nature and concentration of the alcohol and the enzymatic source. The application of PLD catalyzed transformations for the production of a great number of PLs with important uses in medical, nutraceutical and cosmetic sectors will be discussed in this work. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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34 pages, 3661 KiB

Open AccessReview

Main Structural Targets for Engineering Lipase Substrate Specificity

by Samah Hashim Albayati, Malihe Masomian, Siti Nor Hasmah Ishak, Mohd Shukuri bin Mohamad Ali, Adam Leow Thean, Fairolniza binti Mohd Shariff, Noor Dina binti Muhd Noor and Raja Noor Zaliha Raja Abd Rahman

Catalysts 2020, 10(7), 747; https://doi.org/10.3390/catal10070747 - 6 Jul 2020

Cited by 46 | Viewed by 10234

Abstract

Microbial lipases represent one of the most important groups of biotechnological biocatalysts. However, the high-level production of lipases requires an understanding of the molecular mechanisms of gene expression, folding, and secretion processes. Stable, selective, and productive lipase is essential for modern chemical industries, as most lipases cannot work in different process conditions. However, the screening and isolation of a new lipase with desired and specific properties would be time consuming, and costly, so researchers typically modify an available lipase with a certain potential for minimizing cost. Improving enzyme properties is associated with altering the enzymatic structure by changing one or several amino acids in the protein sequence. This review detailed the main sources, classification, structural properties, and mutagenic approaches, such as rational design (site direct mutagenesis, iterative saturation mutagenesis) and direct evolution (error prone PCR, DNA shuffling), for achieving modification goals. Here, both techniques were reviewed, with different results for lipase engineering, with a particular focus on improving or changing lipase specificity. Changing the amino acid sequences of the binding pocket or lid region of the lipase led to remarkable enzyme substrate specificity and enantioselectivity improvement. Site-directed mutagenesis is one of the appropriate methods to alter the enzyme sequence, as compared to random mutagenesis, such as error-prone PCR. This contribution has summarized and evaluated several experimental studies on modifying the substrate specificity of lipases. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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17 pages, 775 KiB

Open AccessReview

The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

by Nur Fathiah Mokhtar, Raja Noor Zaliha Raja Abd. Rahman, Noor Dina Muhd Noor, Fairolniza Mohd Shariff and Mohd Shukuri Mohamad Ali

Catalysts 2020, 10(7), 744; https://doi.org/10.3390/catal10070744 - 4 Jul 2020

Cited by 69 | Viewed by 11067

Abstract

Four major enzymes commonly used in the market are lipases, proteases, amylases, and cellulases. For instance, in both academic and industrial levels, microbial lipases have been well studied for industrial and biotechnological applications compared to others. Immobilization is done to minimize the cost. The improvement of enzyme properties enables the reusability of enzymes and facilitates enzymes used in a continuous process. Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities. Immobilized enzymes can be used repeatedly compared to free enzymes, which are unable to catalyze reactions continuously in the system. Immobilization also provides a higher pH value and thermal stability for enzymes toward synthesis. The main parameter influencing the immobilization is the support used to immobilize the enzyme. The support should have a large surface area, high rigidity, suitable shape and particle size, reusability, and resistance to microbial attachment, which will enhance the stability of the enzyme. The diffusion of the substrate in the carrier is more favorable on hydrophobic supports instead of hydrophilic supports. The methods used for enzyme immobilization also play a crucial role in immobilization performance. The combination of immobilization methods will increase the binding force between enzymes and the support, thus reducing the leakage of the enzymes from the support. The adsorption of lipase on a hydrophobic support causes the interfacial activation of lipase during immobilization. The adsorption method also causes less or no change in enzyme conformation, especially on the active site of the enzyme. Thus, this method is the most used in the immobilization process for industrial applications. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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22 pages, 3254 KiB

Open AccessFeature PaperReview

Stereoselective Synthesis of Terpenoids through Lipase-Mediated Resolution Approaches

by Stefano Serra and Davide De Simeis

Catalysts 2020, 10(5), 504; https://doi.org/10.3390/catal10050504 - 4 May 2020

Cited by 8 | Viewed by 4255

Abstract

This review article focuses on the scientific developments concerning the lipase-mediated synthesis of terpenoids that have been reported in the literature during the last twenty years. More specifically, this review describes in depth the resolution approaches that allow the preparation of the chiral building blocks used for the stereoselective synthesis of bioactive terpenoids. The synthetic methods that have given new and innovative perspectives from a scientific standpoint, and the preparative approaches that possess industrial importance, are described thoroughly. Full article

(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)

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