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Life
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Advances in Research in Biocatalysis: 2nd Edition
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Advances in Research in Biocatalysis: 2nd Edition

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".

Deadline for manuscript submissions: 30 April 2025 | Viewed by 616

Special Issue Editors

Dr. Kari Stone

E-Mail Website
Guest Editor
Department of Chemistry, Lewis University, Romeoville, IL 60446, USA
Interests: biocatalysis; metalloenzymes; bioinorganic; green chemistry; chemical education
Special Issues, Collections and Topics in MDPI journals
Dr. Daniel Kissel

E-Mail Website
Guest Editor
Department of Chemistry, Lewis University, Romeoville, IL 60446, USA
Interests: MOFs; coordination chemistry; materials science
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are grateful to the researchers who contributed to the first volume of this Special Issue “Advances in Research in Biocatalysis”: https://www.mdpi.com/journal/life/special_issues/432U60H35T.

We are pleased to announce the upcoming publication of another Special Issue, entitled “Advances in Research in Biocatalysis: 2nd Edition".

The field of biocatalysis encompasses any type of metabolic transformation, from whole cells to purified enzymes, which produces new compounds that are of interest for industrial applications or environmental remediation purposes. An overarching goal of biocatalysis is to augment or replace many chemical processes by introducing greener alternatives, thus minimizing waste and costs, preventing pollution, and supporting sustainability. Enzymes are becoming more prominent in the production of pharmaceuticals, fragrances, biofuels, and polymers. This Special Issue invites papers from authors that study a broad spectrum of biological, chemical, and engineering topics, including biochemicals, biomedical issues, biomaterials, biocatalysis, the directed evolution of enzymes, biodegradation, biofuels, bioplastics, and environmental remediation. These prospective authors should first send a short abstract or tentative title to the Editorial Office. If the Editors deem the topic appropriate for inclusion in the Special Issue, the author will be encouraged to submit a full manuscript. Please contact the Guest Editors for questions regarding the suitability of your manuscript.

Dr. Kari Stone
Dr. Daniel Kissel
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. Life 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 2600 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

  • biochemical
  • biomedical
  • biomaterials
  • biocatalysis
  • biodegradation
  • biofuels
  • bioplastics
  • directed evolution of enzymes
  • environmental remediation

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Published Papers (1 paper)

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Research

17 pages, 7035 KiB  
Article
Characterization and PCR Application of Family B DNA Polymerases from Thermococcus stetteri
by Aleksandra A. Kuznetsova, Marina A. Soloveva, Elena S. Mikushina, Anastasia A. Gavrilova, Artemiy S. Bakman and Nikita A. Kuznetsov
Life 2024, 14(12), 1544; https://doi.org/10.3390/life14121544 - 25 Nov 2024
Viewed by 328
Abstract
DNA polymerases from the hyperthermophilic Archaea have attracted considerable attention as PCR enzymes due to their high thermal stability and proofreading 3′ → 5′ exonuclease activity. This study is the first to report data concerning the purification and biochemical characteristics of the Tst [...] Read more.
DNA polymerases from the hyperthermophilic Archaea have attracted considerable attention as PCR enzymes due to their high thermal stability and proofreading 3′ → 5′ exonuclease activity. This study is the first to report data concerning the purification and biochemical characteristics of the Tst DNA polymerase from Thermococcus stetteri. Both the wild type Tst(wt) DNA polymerase and its chimeric form containing the P36H substitution—which reduces the enzyme’s affinity for the U-containing template and dUTP—and the DNA-binding domain Sso7d from S. solfataricus were obtained and analyzed. It was shown that Tst(wt) could effectively amplify up to 6-kb DNA fragments, whereas TstP36H–Sso7d could amplify DNA fragments up to 15 kb. It was found that TstP36H–Sso7d has superior PCR efficiency compared to the commonly used DNA polymerase PfuV93Q–Sso7d. For the amplification of a 2-kb DNA fragment, TstP36H–Sso7d required less than 10 s of extension time, whereas for PfuV93Q–Sso7d, the extension time was no less than 30 s. Steady-state kinetic assays revealed that the dNTP-binding affinity KdNTPm was the same for TstP36H–Sso7d and PfuV93Q–Sso7d, whereas the maximum rate of dNTP incorporation, kcat, was two orders of magnitude higher for TstP36H–Sso7d. Moreover, the incorporation of incorrect dNTP was not observed for TstP36H–Sso7d up to 56 °C, whereas for PfuV93Q–Sso7d, the extension of primer with incorrect dNTP was observed at 37 °C, supporting higher fidelity of TstP36H–Sso7d. The obtained data suggest that TstP36H–Sso7d may be a good candidate for high-fidelity DNA amplification. Full article
(This article belongs to the Special Issue Advances in Research in Biocatalysis: 2nd Edition)
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