Results 21 to 30 of about 210,476 (300)

Cold Adaptation of a Mesophilic Subtilisin-like Protease by Laboratory Evolution [PDF]

open access: yes, 2000
Enzymes isolated from organisms native to cold environments generally exhibit higher catalytic efficiency at low temperatures and greater thermosensitivity than their mesophilic counterparts.
Arnold, Frances H.   +2 more
core   +1 more source

Dynamic allostery can drive cold adaptation in enzymes [PDF]

open access: yesNature, 2018
Adaptation of organisms to environmental niches is a hallmark of evolution. One prevalent example is that of thermal adaptation, in which two descendants evolve at different temperature extremes1,2. Underlying the physiological differences between such organisms are changes in enzymes that catalyse essential reactions 3 , with orthologues from each ...
Saavedra, Harry G.   +4 more
openaire   +2 more sources

Characterization of a strain producing cold-adapted protease and enzyme purification

open access: yes浙江大学学报. 农业与生命科学版, 2006
A strain producing cold-adapted protease was isolated from soil and identified, named strain HL221. It was suggested that strain HL221 was the closest relative of Chryseobacterium scophthalmum, based on phylogenetic analysis of 16S rDNA with 99% of ...
LIU Jing   +3 more
doaj   +1 more source

In Vivo Evolution of Butane Oxidation by Terminal Alkane Hydroxylases AlkB and CYP153A6 [PDF]

open access: yes, 2009
Enzymes of the AlkB and CYP153 families catalyze the first step in the catabolism of medium-chain-length alkanes, selective oxidation of the alkane to the 1-alkanol, and enable their host organisms to utilize alkanes as carbon sources.
Arnold, Frances H.   +3 more
core   +3 more sources

Novel cold-adapted raw-starch digesting α-amylases from Eisenia fetida: Gene cloning, expression, and characterization

open access: yesBiotechnology Reports, 2021
We identified the raw-starch-digesting α-amylase genes a earthworm Eisenia fetid α amylase I and II (Ef-Amy I and Ef-Amy II). Each gene consists of 1,530 base pairs (bp) that encode proteins of 510 amino acids, as indicated by the corresponding mRNA ...
Kana Tsukamoto   +4 more
doaj   +1 more source

Study on a Novel Cold-Active and Halotolerant Monoacylglycerol Lipase Widespread in Marine Bacteria Reveals a New Group of Bacterial Monoacylglycerol Lipases Containing Unusual C(A/S)HSMG Catalytic Motifs

open access: yesFrontiers in Microbiology, 2020
Monoacylglycerol lipases (MGLs) are present in all domains of life. However, reports on bacterial MGLs are still limited. Until now, reported bacterial MGLs are all thermophilic/mesophilic enzymes from warm terrestrial environments or deep-sea ...
Ping-Yi Li   +16 more
doaj   +1 more source

Characterization of EstDR4, a Novel Cold-Adapted Insecticides-Metabolizing Esterase from Deinococcus radiodurans

open access: yesApplied Sciences, 2021
Cold-adapted esterases are attracting increasing attention owing to their prospective use in biotechnology. In this study, a novel cold-adapted family Ⅳ esterase EstDR4 was identified and obtained from extremophile Deinococcus radiodurans (D. radiodurans)
Yage Zhang   +7 more
doaj   +1 more source

The genome and transcriptome of Trichormus sp NMC-1: insights into adaptation to extreme environments on the Qinghai-Tibet Plateau [PDF]

open access: yes, 2016
The Qinghai-Tibet Plateau (QTP) has the highest biodiversity for an extreme environment worldwide, and provides an ideal natural laboratory to study adaptive evolution.
A Stamatakis   +53 more
core   +2 more sources

A molecular perspective on the limits of life: Enzymes under pressure [PDF]

open access: yes, 2016
From a purely operational standpoint, the existence of microbes that can grow under extreme conditions, or "extremophiles", leads to the question of how the molecules making up these microbes can maintain both their structure and function. While microbes
Bartlett, D. H.   +5 more
core   +2 more sources

A single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida

open access: yesCurrent Research in Biotechnology, 2023
To improve the specific activity at low temperatures of Ef-EG2 and to maintain thermostability, five mutant enzymes (K273R, N372D, Q387E, N402D, D43R) were produced. The two mutant enzymes (K273R, N402D) lost the cellulase activity.
Chikako Kuroki   +5 more
doaj   +1 more source

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