Special Issue "Novel Enzyme and Whole-Cell Biocatalysis"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: 31 March 2018

Special Issue Editor

Guest Editor
Prof. Dr. Thomas Brück

Technische Universität München (TUM), Department of Chemistry, Head of Industrial Biocatalysis, Raum/Room: CH-27543, Lichtenberg Str. 4, D-85748 Garching bei München, Deutschland/Germany
Website | E-Mail
Phone: +49-89-289-13253
Interests: biocaqtalytic biomass conversion; biocatalytic valorization of biogenic building blocks

Special Issue Information

Dear Colleagues,

The role of catalysis in realizing a sustainable, bioeconomy climate change drives the development of sustainable processes in the chemical industry. In this respect, the utilization of biomass feedstocks is key in realizing a sustainable bioeconomy on a global scale. The conversion of complex biomass resources into value adding products is challenging due to the inherent chemical complexity of these feedstocks. To this end the role of biocatalysts (whole cells or enzymes) is currently the dominant approach to achieve efficient conversion with high selectivity in aqueous reaction media. However, the recent advent of novel solvent systems, such as ionic liquids, and advances in chemical catalyst design now open new conversion routes combining both bio- and chemical catalysis towards conversion and refining of complex biomass into target products. This Special Issue of Catalysts will focus on new catalytic cascades that preferentially combine both bio-catalytic and chemical steps to generate renewable products. Contributions that report on new catalysts or bioprocess engineering solutions particularly using novel solvent or product isolation procedures systems are welcome.

Prof. Dr. Thomas Brück
Guest Editor

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. 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 1300 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

  • biomass conversion
  • catalyst design
  • catalytic cascades
  • chemical catalysts
  • biocatalysts
  • process engineering
  • downstream processing

Published Papers (1 paper)

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Research

Open AccessArticle Over-Expression of the Thermobifida fusca β-Glucosidase in a Yarrowia lipolytica Transformant to Degrade Soybean Isoflavones
Catalysts 2018, 8(1), 24; doi:10.3390/catal8010024
Received: 4 January 2018 / Revised: 12 January 2018 / Accepted: 12 January 2018 / Published: 14 January 2018
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Abstract
A gene (bgl) encoding a β-glucosidase in thermophilic actinomycete Thermobifida fusca NTU 22 was cloned into a Yarrowia lipolytica expression system. Heterologous expression resulted in extracellular β-glucosidase production with activity as high as 630 U/mL in a Hinton flask culture filtrate.
[...] Read more.
A gene (bgl) encoding a β-glucosidase in thermophilic actinomycete Thermobifida fusca NTU 22 was cloned into a Yarrowia lipolytica expression system. Heterologous expression resulted in extracellular β-glucosidase production with activity as high as 630 U/mL in a Hinton flask culture filtrate. This recombinant β-glucosidase was purified 9.2-fold from crude culture filtrate by DEAE-Sepharose FF column chromatography as measured by its increase in specific activity. The overall yield of the purified enzyme was 47.5%. The molecular weight of the purified β-glucosidase estimated by SDS-PAGE was 45 kDa, which agreed with the predicted molecular weight based on the nucleotide sequence. About 15% enzyme activity loss was observed after the enzyme was heat-treated at 50 °C for 180 min. It was also found that the activity of the enzyme was inhibited by Hg2+, Cu2+, Ba2+, Ag+, p-chloromercuribenzene, and iodoacetate. The β-glucosidase from T. fusca had the most activity for daidzein-7-glucoside and genistein-7-glucoside among the tested flavonoid glycosides, but there was moderate or little activity for luteolin-7-glucoside, cyanidine-3-glucoside, and quercetin-3-glucoside. These properties are important for the soybean isoflavone applications of this β-glucosidase. Full article
(This article belongs to the Special Issue Novel Enzyme and Whole-Cell Biocatalysis)
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