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Journals
Catalysts
Special Issues
Biomacromolecules in Non-Conventional Media: Biotransformations and Beyond
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Biomacromolecules in Non-Conventional Media: Biotransformations and Beyond

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

Deadline for manuscript submissions: closed (30 June 2019) | Viewed by 2886

Special Issue Editors

Prof. Dr. Francesco Secundo

E-Mail Website
Guest Editor
CNR, Istituto di Chimica del Riconoscimento Molecolare, I-20131 Milan, Italy
Interests: biocatalysis; protein conformation; analysis of food samples
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Xiangzhao Mao

E-Mail Website
Guest Editor
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
Interests: food enzyme; biocatalysis and biotransformation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Biocatalysis in non-conventional media is a well established procedures that has been extensively developed since the ‘80s. Indeed, organic solvents, supercritical fluids, gases, and ionic liquids have been employed as reaction media for biocatalyzed reactions. However, besides biotransformations, organic media (in particular ionic liquids) are routinely employed for the extraction and/or manipulation of different types of biomacromolecules (e.g., polysaccharides, nucleic acids, proteins). Thus, in addition to new examples on the use of non-aqueous media for reactions catalyzed by enzyme or whole cells, also the effects of organic solvents or ionic liquids on biomacromolecules exploited for the preparation of new products (e.g. nanomaterials) is a topic of actual  interests.

The goal of this themed issue is to report new advancements where using organic solvents, supercritical fluids, gases, or ionic liquids it has been possible to carry out a successful biotransformation, extraction or manipulation of biomacromolecules.

Prof. Francesco Secundo
Prof. Xiangzhao Mao
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 submissions that pass pre-check are 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. Catalysts is an international peer-reviewed open access monthly 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 2700 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

  • organic solvents
  • supercritical fluids
  • gases
  • ionic liquids
  • biomaterials
  • proteins
  • polysaccharides
  • nucleic acids
  • nanoparticles

Published Papers (1 paper)

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Research

12 pages, 1640 KiB  
Article
Cloning, Expression, and Characterization of a Novel Thermostable and Alkaline-stable Esterase from Stenotrophomonas maltophilia OUC_Est10 Catalytically Active in Organic Solvents
by Xinwei Gao, Xiangzhao Mao, Ping Lu, Francesco Secundo, Changhu Xue and Jianan Sun
Catalysts 2019, 9(5), 401; https://doi.org/10.3390/catal9050401 - 29 Apr 2019
Cited by 12 | Viewed by 2477
Abstract
A thermostable and alkaline-stable novel esterase (Est7) was identified through the whole genome sequencing of Stenotrophomonas maltophilia OUC_Est10. The open reading frame of this gene encoded 617 amino acid residues. After heterologous expression in Escherichia coli BL21 (DE3), the purified Est7 was separated [...] Read more.
A thermostable and alkaline-stable novel esterase (Est7) was identified through the whole genome sequencing of Stenotrophomonas maltophilia OUC_Est10. The open reading frame of this gene encoded 617 amino acid residues. After heterologous expression in Escherichia coli BL21 (DE3), the purified Est7 was separated as a single protein and presented a molecular mass of 70.6 kDa. Multiple sequence alignment indicated that Est7 had a typical catalytic triad (Ser-Asp-His) and the conserved sequence (GDSL) typical of the family II lipid hydrolase proteins. Est7 showed good stability in alkaline buffers, especially in Tris-HCl buffer at pH 9.0 (residual activity 93.8% after 96 h at 4 °C) and in the medium temperature conditions (residual activity 70.2% after 96 h at 45 °C and pH 8.0). The enzyme also retained higher stability toward several hydrophilic and hydrophobic organic solvents (e.g., after incubation in 100% acetonitrile or in n-hexane the enzyme retained about 97% and 84% of the activity in the absence of organic solvent, respectively). Furthermore, Est7 could catalyze the transesterification reaction of vinylacetate with 2-phenylethanol and cis-3-hexen-1-ol to their corresponding acetate esters in petroleum ether or tert-butyl methyl ether. These results indicate Est7 as a promising biocatalyst for applications of Est7 in non-aqueous media. Full article
(This article belongs to the Special Issue Biomacromolecules in Non-Conventional Media: Biotransformations and Beyond)
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