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Marine Drugs
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Marine Enzymes: Sources, Biochemistry and Bioprocesses for Marine Biotechnology –...
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Marine Enzymes: Sources, Biochemistry and Bioprocesses for Marine Biotechnology – III

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (20 November 2021) | Viewed by 8210

Special Issue Editor

Dr. Antonio Trincone

E-Mail Website
Guest Editor
Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli, Napoli, Italy
Interests: biocatalysis; marine enzymes; marine glycosidases; marine biotechnology; oligosaccharides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Applied biocatalysis in the wider acceptation benefits from using new marine enzymes. The marine ecosystem as a recognized fount of bioactive substances is also appreciated as a source of enzymes carrying new and surprising catalytic activities. The uniqueness of marine biocatalysts characterizes their bioprocesses and is based on habitat-related properties such as salt tolerance, hyperthermostability, barophilicity, cold adaptivity, etc. However, commercial exploitations in marine biotechnology are not familiar. Moreover, the novelty of marine enzymes is more pervasive; in fact, new characteristics linked to the metabolic functions of the enzymes and to the ecological asset of the natural source can be discovered at the molecular level of catalysis, especially concerning the stereochemistry of products. Sources are represented by marine microorganism, plants, and animals, but great efforts are directed toward extremophiles or symbiotic microorganisms and towards molecular biology tools for discovery. Setting up bioreactors for marine metabolite production is a key point in all fields of marine biotechnology. In this Special Issue, articles or reviews will discuss more recent successes in the investigation of marine biocatalysts covering all fields of applications. Sources of enzymes, marine molecular biology tools, and the study of all applicative aspects of marine biocatalysis will be acknowledged.

As the Guest Editor, I invite researchers from industry and academia working with marine enzymes to describe recent advances in the field.

Dr. Antonio Trincone
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 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. Marine Drugs 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 2900 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

  • Marine biotechnology
  • Marine biocatalysis
  • Marine bioprocesses
  • Biobased production of marine molecules
  • Marine natural products

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Published Papers (3 papers)

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Research

13 pages, 1675 KiB  
Article
ARTP Mutagenesis of Schizochytrium sp. PKU#Mn4 and Clethodim-Based Mutant Screening for Enhanced Docosahexaenoic Acid Accumulation
by Lu Liu, Mohan Bai, Sai Zhang, Jiantao Li, Xianhua Liu, Biswarup Sen and Guangyi Wang
Mar. Drugs 2021, 19(10), 564; https://doi.org/10.3390/md19100564 - 7 Oct 2021
Cited by 14 | Viewed by 2764
Abstract
Schizochytrium species are one of the best oleaginous thraustochytrids for high-yield production of docosahexaenoic acid (DHA, 22:6). However, the DHA yields from most wild-type (WT) strains of Schizochytrium are unsatisfactory for large-scale production. In this study, we applied the atmospheric and room-temperature plasma [...] Read more.
Schizochytrium species are one of the best oleaginous thraustochytrids for high-yield production of docosahexaenoic acid (DHA, 22:6). However, the DHA yields from most wild-type (WT) strains of Schizochytrium are unsatisfactory for large-scale production. In this study, we applied the atmospheric and room-temperature plasma (ARTP) tool to obtain the mutant library of a previously isolated strain of Schizochytrium (i.e., PKU#Mn4). Two rounds of ARTP mutagenesis coupled with the acetyl-CoA carboxylase (ACCase) inhibitor (clethodim)-based screening yielded the mutant A78 that not only displayed better growth, glucose uptake and ACCase activity, but also increased (54.1%) DHA content than that of the WT strain. Subsequent optimization of medium components and supplementation improved the DHA content by 75.5 and 37.2%, respectively, compared with that of mutant A78 cultivated in the unoptimized medium. Interestingly, the ACCase activity of mutant A78 in a medium supplemented with biotin, citric acid or sodium citrate was significantly greater than that in a medium without supplementation. This study provides an effective bioengineering approach for improving the DHA accumulation in oleaginous microbes. Full article
(This article belongs to the Special Issue Marine Enzymes: Sources, Biochemistry and Bioprocesses for Marine Biotechnology – III)
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12 pages, 1381 KiB  
Article
Evaluation of Aqueous Biphasic Electrophoresis System Based on Halide-Free Ionic Liquids for Direct Recovery of Keratinase
by Phei Er Kee, Hip Seng Yim, Akihiko Kondo, John Chi-Wei Lan and Hui Suan Ng
Mar. Drugs 2021, 19(8), 463; https://doi.org/10.3390/md19080463 - 17 Aug 2021
Cited by 1 | Viewed by 2194
Abstract
Aqueous biphasic electrophoresis system (ABES) incorporates electric fields into the biphasic system to separate the target biomolecules from crude feedstock. Ionic liquid (IL) is regarded as an excellent candidate as the phase-forming components for ABES because of the great electrical conductivity, which can [...] Read more.
Aqueous biphasic electrophoresis system (ABES) incorporates electric fields into the biphasic system to separate the target biomolecules from crude feedstock. Ionic liquid (IL) is regarded as an excellent candidate as the phase-forming components for ABES because of the great electrical conductivity, which can promote the electromigration of biomolecules in ABES, and thereby enhances the separation efficiency of the target biomolecules from crude feedstock. The application of electric fields to the conventional biphasic system expedites the phase settling time of the biphasic system, which eases the subsequent scaling-up steps and reduces the overall processing time of the recovery process. Alkyl sulphate-based IL is a green and economical halide-free surfactant when compared to the other halide-containing IL. The feasibility of halide-free IL-based ABES to recover Kytococcus sedentarius TWHK01 keratinase was studied. Optimum partition coefficient (Ke = 7.53 ± 0.35) and yield (YT = 80.36% ± 0.71) were recorded with IL-ABES comprised of 15.0% (w/w) [EMIM][ESO4], 20.0% (w/w) sodium carbonate and 15% (w/w) crude feedstock. Selectivity (S) of 5.75 ± 0.27 was obtained with the IL-ABES operated at operation time of 5 min with 10 V voltage supplied. Halide-free IL is proven to be a potential phase-forming component of IL-ABES for large-scale recovery of keratinase. Full article
(This article belongs to the Special Issue Marine Enzymes: Sources, Biochemistry and Bioprocesses for Marine Biotechnology – III)
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14 pages, 3932 KiB  
Article
Identification and Biochemical Characterization of a Surfactant-Tolerant Chondroitinase VhChlABC from Vibrio hyugaensis LWW-1
by Juanjuan Su, Xiaoyi Wang, Chengying Yin, Yujiao Li, Hao Wu, Wengong Yu and Feng Han
Mar. Drugs 2021, 19(7), 399; https://doi.org/10.3390/md19070399 - 18 Jul 2021
Cited by 2 | Viewed by 2396
Abstract
Chondroitinases, catalyzing the degradation of chondroitin sulfate (CS) into oligosaccharides, not only play a crucial role in understanding the structure and function of CS, but also have been reported as a potential candidate drug for the treatment of high CS-related diseases. Here, a [...] Read more.
Chondroitinases, catalyzing the degradation of chondroitin sulfate (CS) into oligosaccharides, not only play a crucial role in understanding the structure and function of CS, but also have been reported as a potential candidate drug for the treatment of high CS-related diseases. Here, a marine bacterium Vibrio hyugaensis LWW-1 was isolated, and its genome was sequenced and annotated. A chondroitinase, VhChlABC, was found to belong to the second subfamily of polysaccharide lyase (PL) family 8. VhChlABC was recombinant expressed and characterized. It could specifically degrade CS-A, CS-B, and CS-C, and reached the maximum activity at pH 7.0 and 40 °C in the presence of 0.25 M NaCl. VhChlABC showed high stability within 8 h under 37 °C and within 2 h under 40 °C. VhChlABC was stable in a wide range of pH (5.0~10.6) at 4 °C. Unlike most chondroitinases, VhChlABC showed high surfactant tolerance, which might provide a good tool for removing extracellular CS proteoglycans (CSPGs) of lung cancer under the stress of pulmonary surfactant. VhChlABC completely degraded CS to disaccharide by the exolytic mode. This research expanded the research and application system of chondroitinases. Full article
(This article belongs to the Special Issue Marine Enzymes: Sources, Biochemistry and Bioprocesses for Marine Biotechnology – III)
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