Helping proteins come in from the cold: 5 burning questions about cold-active enzymes

Jan Stanislaw Nowak; Daniel E Otzen

doi:10.1016/j.bbadva.2023.100104

Helping proteins come in from the cold: 5 burning questions about cold-active enzymes

Jan Stanislaw Nowak, Daniel E Otzen

Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Review › Forskning › peer review

Abstract

Enzymes from psychrophilic (cold-loving) organisms have attracted considerable interest over the past decades for their potential in various low-temperature industrial processes. However, we still lack large-scale commercialization of their activities. Here, we review their properties, limitations and potential. Our review is structured around answers to 5 central questions: 1. How do cold-active enzymes achieve high catalytic rates at low temperatures? 2. How is protein flexibility connected to cold-activity? 3. What are the sequence-based and structural determinants for cold-activity? 4. How does the thermodynamic stability of psychrophilic enzymes reflect their cold-active capabilities? 5. How do we effectively identify novel cold-active enzymes, and can we apply them in an industrial context? We conclude that emerging screening technologies combined with big-data handling and analysis make it reasonable to expect a bright future for our understanding and exploitation of cold-active enzymes.

Originalsprog	Engelsk
Artikelnummer	100104
Tidsskrift	BBA advances
Vol/bind	5
ISSN	2667-1603
DOI	https://doi.org/10.1016/j.bbadva.2023.100104
Status	Udgivet - 2024

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10.1016/j.bbadva.2023.100104Licens: CC BY-NC-ND

Citationsformater

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abstract = "Enzymes from psychrophilic (cold-loving) organisms have attracted considerable interest over the past decades for their potential in various low-temperature industrial processes. However, we still lack large-scale commercialization of their activities. Here, we review their properties, limitations and potential. Our review is structured around answers to 5 central questions: 1. How do cold-active enzymes achieve high catalytic rates at low temperatures? 2. How is protein flexibility connected to cold-activity? 3. What are the sequence-based and structural determinants for cold-activity? 4. How does the thermodynamic stability of psychrophilic enzymes reflect their cold-active capabilities? 5. How do we effectively identify novel cold-active enzymes, and can we apply them in an industrial context? We conclude that emerging screening technologies combined with big-data handling and analysis make it reasonable to expect a bright future for our understanding and exploitation of cold-active enzymes.",

keywords = "Bioprospecting, Enzyme catalysis, Protein dynamics, Psychrophilicity, Thermodynamic stability",

author = "Nowak, {Jan Stanislaw} and Otzen, {Daniel E}",

note = "{\textcopyright} 2023 The Authors. Published by Elsevier B.V.",

year = "2024",

doi = "10.1016/j.bbadva.2023.100104",

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T1 - Helping proteins come in from the cold

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AU - Nowak, Jan Stanislaw

AU - Otzen, Daniel E

PY - 2024

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N2 - Enzymes from psychrophilic (cold-loving) organisms have attracted considerable interest over the past decades for their potential in various low-temperature industrial processes. However, we still lack large-scale commercialization of their activities. Here, we review their properties, limitations and potential. Our review is structured around answers to 5 central questions: 1. How do cold-active enzymes achieve high catalytic rates at low temperatures? 2. How is protein flexibility connected to cold-activity? 3. What are the sequence-based and structural determinants for cold-activity? 4. How does the thermodynamic stability of psychrophilic enzymes reflect their cold-active capabilities? 5. How do we effectively identify novel cold-active enzymes, and can we apply them in an industrial context? We conclude that emerging screening technologies combined with big-data handling and analysis make it reasonable to expect a bright future for our understanding and exploitation of cold-active enzymes.

AB - Enzymes from psychrophilic (cold-loving) organisms have attracted considerable interest over the past decades for their potential in various low-temperature industrial processes. However, we still lack large-scale commercialization of their activities. Here, we review their properties, limitations and potential. Our review is structured around answers to 5 central questions: 1. How do cold-active enzymes achieve high catalytic rates at low temperatures? 2. How is protein flexibility connected to cold-activity? 3. What are the sequence-based and structural determinants for cold-activity? 4. How does the thermodynamic stability of psychrophilic enzymes reflect their cold-active capabilities? 5. How do we effectively identify novel cold-active enzymes, and can we apply them in an industrial context? We conclude that emerging screening technologies combined with big-data handling and analysis make it reasonable to expect a bright future for our understanding and exploitation of cold-active enzymes.

KW - Bioprospecting

KW - Enzyme catalysis

KW - Protein dynamics

KW - Psychrophilicity

KW - Thermodynamic stability

U2 - 10.1016/j.bbadva.2023.100104

DO - 10.1016/j.bbadva.2023.100104

M3 - Review

C2 - 38162634

SN - 2667-1603

VL - 5

JO - BBA advances

JF - BBA advances

M1 - 100104

ER -

Helping proteins come in from the cold: 5 burning questions about cold-active enzymes

Abstract

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