Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
4.5
2.7
Journals
Applied Sciences
Special Issues
Cold-Active Proteins and Enzymes
share announcement

Cold-Active Proteins and Enzymes

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 7288

Special Issue Editor

Prof. Dr. Hak Jun Kim

E-Mail Website
Guest Editor
Department of Chemistry, Pukyong National University, Busan 48513, Republic of Korea
Interests: cold-active enzymes; psychrophilic proteins; ice-binding proteins; antifreeze proteins; cold-adaptation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cold-active proteins are characterized by a high catalytic activity and rapid inactivation as low as 30°C. Since the unique feature of cold-active proteins has drawn significant interest from academia and industry over the last few decades, the understanding of cold-active proteins has been ever-increasing. However, the mechanism of the cold adaptation is still not fully illustrated. Cold-adapted organisms or psychrophiles thriving at near- or sub-zero temperatures are repository of cold-active proteins. Hence, worldwide attempts have been made recently to dig out novel cold-active proteins from the Earth's cryobiosphere, which occupies about 80% of our ecosystem. Cold-active proteins, such as proteases and lipases, also have a more significant biotechnological potential compared to their thermophilic counterparts. To utilize their advantages, currently, studies to improve production yield, substrate specificity, and thermostability using fermentation, expression systems including chaperones, site-directed mutagens, molecular dynamics simulation, and structural studies at atomic level are actively ongoing.

This Special Issue, "Cold-active Proteins and Enzymes", of Applied Sciences will cover but is not limited to reviews and recent results regarding the isolation, characterization, engineering, optimization of fermentation of proteases and lipases, structure determination, and applications.

Prof. Dr. Hak Jun Kim
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. Applied Sciences 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 2400 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

  • Cold-active proteases
  • Cold-active lipase
  • Cold-adapted protein
  • Psychrophile
  • Folding
  • Stability
  • Expression system
  • Chaperone
  • Protein design and engineering
  • Crystal structure
  • NMR solution structure
  • Site-directed mutagenesis
  • Microevolution
  • Metagenomics
  • Molecular dynamics simulation
  • Enzyme kinetics
  • Synthetic biology
  • Industrial enzymes
  • Fermentation
  • Applications

Published Papers (2 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Other

15 pages, 3659 KiB  
Article
Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity
by Shweta Bharat Borkar, Sondavid K. Nandanwar, Jun Hyuck Lee and Hak Jun Kim
Appl. Sci. 2019, 9(20), 4299; https://doi.org/10.3390/app9204299 - 13 Oct 2019
Cited by 6 | Viewed by 3203
Abstract
Liver-expressed antimicrobial peptides (LEAPs) are cysteine-containing cationic peptides. LEAP-1 and LEAP-2 are eight- and four-cysteine containing antimicrobial peptides found in animals, respectively. LEAP-1 is widely known as antibacterial peptide involved in the innate immunity of fish, but the roles of LEAP-1 and LEAP-2 [...] Read more.
Liver-expressed antimicrobial peptides (LEAPs) are cysteine-containing cationic peptides. LEAP-1 and LEAP-2 are eight- and four-cysteine containing antimicrobial peptides found in animals, respectively. LEAP-1 is widely known as antibacterial peptide involved in the innate immunity of fish, but the roles of LEAP-1 and LEAP-2 in Antarctic fish species are unknown. In the present study, we synthesized and characterized novel LEAPs with four and eight cysteine residues, derived from Antarctic notothenioid (Dissostichus mawsoni) and Antarctic eelpout (Lycodichthys dearborni). Circular dichroism spectroscopy of these peptides showed a typical β-sheet conformation. The LEAPs were found to be bactericidal against gram-positive as well as gram-negative bacteria. In the SYTOX green uptake assay, LEAPs did not trigger any significant increase in fluorescence. However, LEAPs competitively bound to DNA and replaced the ethidium bromide (EB) dye. To determine the effect of temperature on the activity of LEAPs, we evaluated the antibacterial activity against Listeria monocytogenes at 5, 15, 25, and 35 °C. The results showed that the antibacterial activity of LEAPs increased with a decrease in temperature, which may indicate that the Antarctic fish LEAP are evolutionarily adapted. Taken together, our results suggest that novel Antarctic LEAPs are bactericidal peptides with the likely mode of action being DNA binding and may be evolved to adapt to cold temperature. Full article
(This article belongs to the Special Issue Cold-Active Proteins and Enzymes)
►▼ Show Figures

Figure 1

Other

Jump to: Research

18 pages, 987 KiB  
Perspective
Taking Advantage of Promiscuity of Cold-Active Enzymes
by Sondavid K. Nandanwar, Shweta Bharat Borkar, Jun Hyuck Lee and Hak Jun Kim
Appl. Sci. 2020, 10(22), 8128; https://doi.org/10.3390/app10228128 - 17 Nov 2020
Cited by 9 | Viewed by 3416
Abstract
Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they [...] Read more.
Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology. Full article
(This article belongs to the Special Issue Cold-Active Proteins and Enzymes)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-2
Back to TopTop