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Special Issue "Lipases and Lipases Modification 2019"

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

Deadline for manuscript submissions: closed (15 October 2019).

Special Issue Editors

Dr. Marco Filice
Website
Guest Editor
Nanobiotechnology for Life Sciences Lab., Department of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Universidad Complutense de Madrid (UCM), Spain
Interests: cancer nanomedicine; multifunctional nanotheranostics development; multimodal molecular bioimaging; breast cancer; in vitro and in vivo evaluation of multifunctional nanodrugs; non-viral miRNA delivery; nanobiotechnology;targeted and controlled drug delivery
Dr. Marzia Marciello
Website
Guest Editor
Nanobiotechnology For Life Science Lab (NANOBIOTECH4LS), Dept. of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Compliutense University of Madrid (UCM), Madrid, Spain
Interests: nano-biotechnology; pharmaceutical technology; molecular diagnostic; bio-nanocatalysis
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

As result of decades of studies and applications, nowadays, lipases can be undoubtedly considered as one of the most promising biocatalysts contributing to the development of bio-based industries.

Their ability to catalyze reactions in both aqueous and solvent environments with high efficiency and stability; their chemo-, regio-, and enantioselectivity without cofactors requirement; as well as their countless number of accepted substrates make lipases very attractive and versatile enzymes from an industrial point of view.

In parallel to the description of a myriad of novel lipase-based biotrasformations, even the development of protocols aiming to enhance their catalytic properties have undergone impressive growth. Strategies based on site-targeted chemical modification, controlled immobilization on solid supports, molecular biology, or combinations thereof have proved to be the most important ways to enhance the catalytic properties of lipase biocatalysts. Moreover, the fine fusion of these strategies, together with nanotechnology and bioinformatic technology, has recently opened new multidisciplinary avenues permitting one to further strengthen lipase properties and widen their application scope.

In this Special Issue, we aim to gather contributions illustrating the recent advances in this continuously evolving area. These include but are not restricted to the development of novel lipase-based biotrasformations, new modification strategies, advanced immobilization protocols on different support classes, and the integration of lipases into enzymatic or hybrid multicatalytic cascades.

Dr. Marco Filice
Dr. Marzia Marciello
Guest Editors

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lipase
  • enzyme immobilization
  • biocatalysis
  • nanotechnology
  • protein chemical modification
  • molecular biology
  • biochemistry
  • multicatalytic systems

Published Papers (3 papers)

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Research

Open AccessArticle
Fine Modulation of the Catalytic Properties of Rhizomucor miehei Lipase Driven by Different Immobilization Strategies for the Selective Hydrolysis of Fish Oil
Molecules 2020, 25(3), 545; https://doi.org/10.3390/molecules25030545 - 27 Jan 2020
Cited by 2
Abstract
Functional properties of each enzyme strictly depend on immobilization protocol used for linking enzyme and carrier. Different strategies were applied to prepare the immobilized derivatives of Rhizomucor miehei lipase (RML) and chemically aminated RML (NH2-RML). Both RML and NH2-RML [...] Read more.
Functional properties of each enzyme strictly depend on immobilization protocol used for linking enzyme and carrier. Different strategies were applied to prepare the immobilized derivatives of Rhizomucor miehei lipase (RML) and chemically aminated RML (NH2-RML). Both RML and NH2-RML forms were covalently immobilized on glyoxyl sepharose (Gx-RML and Gx-NH2-RML), glyoxyl sepharose dithiothreitol (Gx-DTT-RML and Gx-DTT-NH2-RML), activated sepharose with cyanogen bromide (CNBr-RML and CNBr-NH2-RML) and heterofunctional epoxy support partially modified with iminodiacetic acid (epoxy-IDA-RML and epoxy-IDA-NH2-RML). Immobilization varied from 11% up to 88% yields producing specific activities ranging from 0.5 up to 1.9 UI/mg. Great improvement in thermal stability for Gx-DTT-NH2-RML and epoxy-IDA-NH2-RML derivatives was obtained by retaining 49% and 37% of their initial activities at 70 °C, respectively. The regioselectivity of each derivative was also examined in hydrolysis of fish oil at three different conditions. All the derivatives were selective between cis-5,8,11,14,17-eicosapentaenoic acid (EPA) and cis-4,7,10,13,16,19-docosahexaenoic acid (DHA) in favor of EPA. The highest selectivity (32.9 folds) was observed for epoxy-IDA-NH2-RML derivative in the hydrolysis reaction performed at pH 5 and 4 °C. Recyclability study showed good capability of the immobilized biocatalysts to be used repeatedly, retaining 50–91% of their initial activities after five cycles of the reaction. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification 2019)
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Open AccessArticle
Lipase-Catalyzed Chemoselective Ester Hydrolysis of Biomimetically Coupled Aryls for the Synthesis of Unsymmetric Biphenyl Esters
Molecules 2019, 24(23), 4272; https://doi.org/10.3390/molecules24234272 - 23 Nov 2019
Abstract
Lipases are among the most frequently used biocatalysts in organic synthesis, allowing numerous environmentally friendly and inexpensive chemical transformations. Here, we present a biomimetic strategy based on iron(III)-catalyzed oxidative coupling and selective ester monohydrolysis using lipases for the synthesis of unsymmetric biphenyl-based esters [...] Read more.
Lipases are among the most frequently used biocatalysts in organic synthesis, allowing numerous environmentally friendly and inexpensive chemical transformations. Here, we present a biomimetic strategy based on iron(III)-catalyzed oxidative coupling and selective ester monohydrolysis using lipases for the synthesis of unsymmetric biphenyl-based esters under mild conditions. The diverse class of biphenyl esters is of pharmaceutical and technical relevance. We explored the potency of a series of nine different lipases of bacterial, fungal, and mammalian origin on their catalytic activities to cleave biphenyl esters, and optimized the reaction conditions, in terms of reaction time, temperature, pH, organic solvent, and water–organic solvent ratios, to improve the chemoselectivity, and hence control the ratio of unsymmetric versus symmetric products. Elevated temperature and increased DMSO content led to an almost exclusive monohydrolysis by the four lipases Candida rugosa lipase (CRL), Mucor miehei lipase (MML), Rhizopus niveus lipase (RNL), and Pseudomonas fluorescens lipase (PFL). The study was complemented by in silico binding predictions to rationalize the observed differences in efficacies of the lipases to convert biphenyl esters. The optimized reaction conditions were transferred to the preparative scale with high yields, underlining the potential of the presented biomimetic approach as an alternative strategy to the commonly used transition metal-based strategies for the synthesis of diverse biphenyl esters. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification 2019)
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Open AccessArticle
Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
Molecules 2019, 24(7), 1313; https://doi.org/10.3390/molecules24071313 - 03 Apr 2019
Cited by 3
Abstract
The recombinant lipase from Ophiostoma piceae OPEr has demonstrated to have catalytic properties superior to those of many commercial enzymes. Enzymatic crudes with OPEr were immobilized onto magnetite nanoparticles by hydrophobicity (SiMAG-Octyl) and by two procedures that involve covalent attachment of the protein [...] Read more.
The recombinant lipase from Ophiostoma piceae OPEr has demonstrated to have catalytic properties superior to those of many commercial enzymes. Enzymatic crudes with OPEr were immobilized onto magnetite nanoparticles by hydrophobicity (SiMAG-Octyl) and by two procedures that involve covalent attachment of the protein (mCLEAs and AMNP-GA), giving three nanobiocatalysts with different specific activity in hydrolysis of p-nitrophenyl butyrate (pNPB) and good storage stability at 4 °C over a period of 4 months. Free OPEr and the different nanobiocatalysts were compared for the synthesis of butyl esters of volatile fatty acids C4 to C7 in reactions containing the same lipase activity. The esterification yields and the reaction rates obtained with AMNP-GA-OPEr were in general higher or similar to those observed for the free enzyme, the mCLEAs-OPEr, and the non-covalent preparation SiMAG-Octyl-OPEr. The time course of the esterification of the acids C4 to C6 catalyzed by AMNP-GA-OPEr was comparable. The synthesis of the C7 ester was slower but very efficient, admitting concentrations of heptanoic acid up to 1 M. The best 1-butanol: acid molar ratio was 2:1 for all the acids tested. Depending on the substrate, this covalent preparation of OPEr maintained 80–96% activity over 7 cycles, revealing its excellent properties, easy recovery and recycling, and its potential to catalyze the green synthesis of chemicals of industrial interest. Full article
(This article belongs to the Special Issue Lipases and Lipases Modification 2019)
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