2020
DOI: 10.3390/app10228128
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Taking Advantage of Promiscuity of Cold-Active Enzymes

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 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 … Show more

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Cited by 17 publications
(13 citation statements)
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“…Over the last 20 years, the interest in cold-adapted microorganisms as a source of new enzymes for industrial processes has intensely grown [ 170 , 171 , 172 ]. Nowadays, a considerable number of industrial processes and products take advantage of microbial enzymes [ 173 , 174 ].…”
Section: Biotechnological Potential Of Fungi Inhabiting Marine Antarctic Environmentsmentioning
confidence: 99%
“…Over the last 20 years, the interest in cold-adapted microorganisms as a source of new enzymes for industrial processes has intensely grown [ 170 , 171 , 172 ]. Nowadays, a considerable number of industrial processes and products take advantage of microbial enzymes [ 173 , 174 ].…”
Section: Biotechnological Potential Of Fungi Inhabiting Marine Antarctic Environmentsmentioning
confidence: 99%
“…5 °C), Mn 2+ might stabilize the ES complex, by optimizing the ES interactions, as suggested by the marked increase of substrate affinity (Table 2). Note that cold-active enzymes often improve activity at low temperatures at the expense of substrate affinity and specificity [7,9,12,33]. On the other hand, at sub-optimal temperatures (i.e.…”
Section: Discussionmentioning
confidence: 99%
“…Whatever the adaptive strategy within a protein family, adaptation usually results in higher conformational flexibility involving the whole protein or a large region of it [4,5,[8][9][10]. Flexibility results in a lower activation energy which allows the catalyst to overcome the cold-induced reduction of the catalytic rate and is often (though not always) accompanied by low thermal stability, a larger temperature gap between the optimum catalysis temperature (T opt ) and the melting temperature (T m ) and low affinity for substrates [5,8,9,11,12]. The discovery of atypical coldactive enzymes (e.g.…”
Section: Introductionmentioning
confidence: 99%
“…These enzymes could be an attractive targets for the biodegradation of bioplastic as well as other industrial applications. Cold-adapted enzymes have a few advantages over mesophilic orthologs in that they operate at low temperature, could reduce the energy cost in the reaction and attenuate side-reactions and they could be easily inactivated by heat (Nandanwar et al 2020 ).…”
Section: Discussionmentioning
confidence: 99%