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Marine Drugs
Special Issues
Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms
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Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms

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

Deadline for manuscript submissions: closed (15 December 2020) | Viewed by 14450

Special Issue Editors

Prof. Dr. Marina Lotti

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Guest Editor
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy
Dr. Marco Mangiagalli

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Guest Editor
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy

Special Issue Information

Dear Colleagues,

Cold environments host a surprising biodiversity and are an amazing source of bioactive molecules with particular properties evolved by organisms to cope with physiological stresses they experience in the cold.

This Special Issue focuses on two major adaptive strategies evolved by marine cold-adapted organisms: enzymes active at low temperature allowing efficient catalysis at low temperature, and ice-binding proteins (IBPs) that counteract the formation of ice crystals. Physiological and mechanistic issues will be tackled, as well as possible technological applications with particular attention paid to their relevance to human health, for example in the cryopreservation of tissue and organs, and lifestyle (e.g., food processing and preservation).

Prof. Dr. Marina Lotti
Dr. Marco Mangiagalli
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. 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.

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Published Papers (4 papers)

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Research

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16 pages, 17854 KiB  
Article
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation
by Guang Yang, Matteo Mozzicafreddo, Patrizia Ballarini, Sandra Pucciarelli and Cristina Miceli
Mar. Drugs 2021, 19(2), 67; https://doi.org/10.3390/md19020067 - 27 Jan 2021
Cited by 12 | Viewed by 2363
Abstract
Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes [...] Read more.
Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic Euplotes focardii and the mesophilic Euplotes crassus. By applying bioinformatics approaches, we compared amino acid composition and predicted secondary and tertiary structures of these lipases to extract relevant information relative to cold adaptation. Our results not only confirm the importance of several previous recognized amino acid substitutions for cold adaptation, as the preference for small amino acid, but also identify some new factors correlated with the secondary structure possibly responsible for enhanced enzyme activity at low temperatures. This study emphasizes the subtle sequence and structural modifications that may help to transform mesophilic into psychrophilic enzymes for industrial applications by protein engineering. Full article
(This article belongs to the Special Issue Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms)
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11 pages, 1532 KiB  
Communication
Protection of Alcohol Dehydrogenase against Freeze–Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property
by Young Hoon Lee, Kitae Kim, Jun Hyuck Lee and Hak Jun Kim
Mar. Drugs 2020, 18(12), 638; https://doi.org/10.3390/md18120638 - 13 Dec 2020
Cited by 3 | Viewed by 2787
Abstract
Ice-binding proteins (IBPs) have ice recrystallization inhibition (IRI) activity. IRI property has been extensively utilized for the cryopreservation of different types of cells and tissues. Recent reports demonstrated that IRI can also play a significant role in protecting proteins from freezing damage during [...] Read more.
Ice-binding proteins (IBPs) have ice recrystallization inhibition (IRI) activity. IRI property has been extensively utilized for the cryopreservation of different types of cells and tissues. Recent reports demonstrated that IRI can also play a significant role in protecting proteins from freezing damage during freeze–thaw cycles. In this study, we hypothesized that the protective capability of IBPs on proteins against freeze–thaw damage is proportional to their IRI activity. Hence we used two IBPs: one with higher IRI activity (LeIBP) and the other with lower activity (FfIBP). Yeast alcohol dehydrogenase (ADH) was used as a freeze-labile model protein. IBPs and ADH were mixed, frozen at −20 °C, and thawed repeatedly. The structure of ADH was assessed using fluorescence emission spectra probed by 1-anilinonaphthalene-8-sulfonate over the repeated freeze–thaw cycles. The activity was monitored at 340 nm spectrophotometrically. Fluorescence data and activity clearly indicated that ADH without IBP was freeze-labile. However, ADH maintained about 70% residual activity after five repeated cycles at a minimal concentration of 0.1 mg mL-1 of high IRI-active LeIBP, but only 50% activity at 4 mg mL−1 of low active FfIBP. These results showed that the protection of proteins from freeze–thaw stress by IBPs is proportional to their IRI activity. Full article
(This article belongs to the Special Issue Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms)
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18 pages, 2298 KiB  
Article
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature
by Marco Orlando, Sandra Pucciarelli and Marina Lotti
Mar. Drugs 2020, 18(11), 579; https://doi.org/10.3390/md18110579 - 20 Nov 2020
Cited by 13 | Viewed by 3800
Abstract
Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins’ sequence and structural organization that result in high conformational flexibility. As a [...] Read more.
Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins’ sequence and structural organization that result in high conformational flexibility. As a consequence of flexibility, several such enzymes are inherently heat sensitive. Cold-active enzymes are of interest for application in a number of bioprocesses, where cold activity coupled with easy thermal inactivation can be of advantage. We describe the biochemical and functional properties of two glycosyl hydrolases (named LYS177 and LYS188) of family 19 (GH19), identified in the genome of an Antarctic marine Pseudomonas. Molecular evolutionary analysis placed them in a group of characterized GH19 endolysins active on lysozyme substrates, such as peptidoglycan. Enzyme activity peaks at about 25–35 °C and 40% residual activity is retained at 5 °C. LYS177 and LYS188 are thermolabile, with Tm of 52 and 45 °C and half-lives of 48 and 12 h at 37 °C, respectively. Bioinformatics analyses suggest that low heat stability may be associated to temperature-driven increases in local flexibility occurring mainly in a specific region of the polypeptide that is predicted to contain hot spots for aggregation. Full article
(This article belongs to the Special Issue Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms)
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Review

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19 pages, 4151 KiB  
Review
Cold-Active β-Galactosidases: Insight into Cold Adaptation Mechanisms and Biotechnological Exploitation
by Marco Mangiagalli and Marina Lotti
Mar. Drugs 2021, 19(1), 43; https://doi.org/10.3390/md19010043 - 19 Jan 2021
Cited by 40 | Viewed by 4784
Abstract
β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied [...] Read more.
β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active β-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries. Full article
(This article belongs to the Special Issue Enzymes and Ice Binding Proteins from Marine Cold-Adapted Organisms)
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