Results 11 to 20 of about 3,703 (125)

Discovery of a cryptic aminoacidic triad involved in the temperature adaptation of GH1 enzymes. [PDF]

open access: yesFEBS J
Cold‐active enzymes retain high catalytic activity at low temperatures but are characterized by thermal instability, a behavior not fully understood. Comparison between a cold‐active GH1 and its mesophilic counterparts highlights the role of a three‐residue motif (W‐M‐F) in conferring structural stability to a mesophilic GH1.
Digiovanni S   +5 more
europepmc   +2 more sources

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

open access: yesMarine Drugs, 2021
Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts.
Guang Yang   +4 more
doaj   +1 more source

Comprehensive insights on environmental adaptation strategies in Antarctic bacteria and biotechnological applications of cold adapted molecules

open access: yesFrontiers in Microbiology, 2023
Climate change and the induced environmental disturbances is one of the major threats that have a strong impact on bacterial communities in the Antarctic environment.
Kesava Priyan Ramasamy   +5 more
doaj   +1 more source

Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes. [PDF]

open access: yesProtein Sci
Abstract The increase in enzyme‐catalyzed reaction rates with temperature is typically modeled using Arrhenius or Eyring relations. Interpretation of extracted parameters is subject to multiple caveats. Here we analyze the impact of temperature variations of underlying activation or Eyring parameters and of temperature‐dependent contributions to ...
McLeod MJ, Thorne RE.
europepmc   +2 more sources

The Sensory, Chemical and Microbiological Quality of Sous-Vide Cooked Sea Bass (<i>Dicentrarchus labrax</i> Linneaus, 1758) With Liquid Smoke Flavor. [PDF]

open access: yesFood Sci Nutr
The processing of sea bass fillets, flavored with liquid smoke‐salt‐vegetable oil, using sous‐vide technology is an innovative method that both enhances organoleptic quality and ensures safe preservation. The fillets, which were flavored and vacuum‐sealed, were cooked at different temperatures and then transferred to cold storage following rapid ...
Köklü R   +5 more
europepmc   +2 more sources

Molecular characterization of cold adaptation of membrane proteins in the Vibrionaceae core-genome. [PDF]

open access: yesPLoS ONE, 2012
Cold-adaptation strategies have been studied in multiple psychrophilic organisms, especially for psychrophilic enzymes. Decreased enzyme activity caused by low temperatures as well as a higher viscosity of the aqueous environment require certain ...
Tim Kahlke, Steinar Thorvaldsen
doaj   +1 more source

Cold-Active β-Galactosidases: Insight into Cold Adaptation Mechanisms and Biotechnological Exploitation

open access: yesMarine Drugs, 2021
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.
Marco Mangiagalli, Marina Lotti
doaj   +1 more source

Cold-Active Enzymes and Their Potential Industrial Applications—A Review

open access: yesMolecules, 2022
More than 70% of our planet is covered by extremely cold environments, nourishing a broad diversity of microbial life. Temperature is the most significant parameter that plays a key role in the distribution of microorganisms on our planet.
Burhan Hamid   +10 more
doaj   +1 more source

Structure analysis of a new psychrophilic marine protease. [PDF]

open access: yesPLoS ONE, 2011
A new psychrophilic marine protease was found from a marine bacterium Flavobacterium YS-80 in the Chinese Yellow Sea. The protease is about 49 kD with an isoelectric point about 4.5.
Si-Cai Zhang   +8 more
doaj   +1 more source

Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles’ Heel in Protein Structure and Industrial Utilization

open access: yesMolecules, 2021
Understanding protein stability is critical for the application of enzymes in biotechnological processes. The structural basis for the stability of thermally adapted chitinases has not yet been examined.
Dale L. Ang   +8 more
doaj   +1 more source

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