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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: 15 October 2019

Special Issue Editors

Guest Editor
Dr. Marco Filice

Nanobiotechnology for Life Sciences Group. Department of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Universidad Complutense de Madrid, Madrid, Spain
Website | E-Mail
Interests: nanobiotechnology; biocatalysis; lipase; bioorganic chemistry; medicinal chemistry; molecular imaging; surface and colloid chemistry; protein chemistry
Guest Editor
Dr. Marzia Marciello

Nanobiotechnology for Life Sciences Group. Department of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Universidad Complutense de Madrid, Madrid, Spain
Website | E-Mail
Interests: biomaterials; pharmaceutical technology; bioorganic chemistry; lipase; nano-biotechnology; chemistry and technology of advanced materials

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

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 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 (1 paper)

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Research

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
Received: 5 March 2019 / Revised: 29 March 2019 / Accepted: 2 April 2019 / Published: 3 April 2019
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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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