Erlend Kristiansen

Roskilde University

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Sindre Andre Pedersen

NTNU Samfunnsforskning

K. E. Zachariassen

Norwegian University of Science and Technology

Karl Erik Zachariassen

Norwegian University of Science and Technology

Hans Ramløv

Roskilde University

Olav Egeland

Norwegian University of Science and Technology

R.A. Andersen

Oslo University Hospital

Dennis Steven Friis

Roskilde University

ÅH

Åsmund Hjulstad

Equinor (United Kingdom)

A. E. Laugsand

Norwegian Institute for Nature Research

N. G. Li

Institute of Zoology

Cooperative Institutions

Norwegian University of Science and Technology

Technical University of Denmark

Roskilde University

University of Copenhagen

University of Oslo

Norwegian Institute for Nature Research

University of Southern Denmark

Aarhus University

University of British Columbia

Scripps Institution of Oceanography

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Ice Nucleation and Antinucleation in Nature

Cryobiology (2000)

Karl Erik Zachariassen Erlend Kristiansen

Supercooling

Ectotherm

Ice nucleus

Antifreeze protein

Clear ice

10.1006/cryo.2000.2289

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Citations (397)

Antifreeze activity enhancement by site directed mutagenesis on an antifreeze protein from the beetle Rhagium mordax

FEBS Letters (2014)

Dennis Steven Friis Erlend Kristiansen Nicolas von Solms Hans Ramløv

The ice binding motifs of insect antifreeze proteins (AFPs) mainly consist of repetitive TxT motifs aligned on a flat face of the protein. However, these motifs often contain non‐threonines that disrupt the TxT pattern. We substituted two such disruptive amino acids located in the ice binding face of an AFP from Rhagium mordax with threonine. Furthermore, a mutant with an extra ice facing TxT motif was constructed. These mutants showed enhanced antifreeze activity compared to the wild type at low concentrations. However, extrapolating the data indicates that the wild type will become the most active at concentrations above 270 μmol.

Antifreeze protein

Antifreeze

10.1016/j.febslet.2014.03.032

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Citations (20)

State-space representation of radiation forces in time-domain vessel models

Ocean Engineering (2005)

Erlend Kristiansen Åsmund Hjulstad Olav Egeland

Representation

Convolution (computer science)

State-space representation

10.1016/j.oceaneng.2005.02.009

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Citations (132)

Effect of ice fraction and dilution factor on the antifreeze activity in the hemolymph of the cerambycid beetle Rhagium inquisitor

Cryobiology (2002)

Karl Erik Zachariassen Arthur L. DeVries Ben Hunt Erlend Kristiansen

Dilution

Hemolymph

Antifreeze protein

Hysteresis

Mass fraction

Antifreeze

10.1016/s0011-2240(02)00014-7

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Citations (28)

The Siberian timberman Acanthocinus aedilis: a freeze-tolerant beetle with low supercooling points

Journal of Comparative Physiology B (2009)

Erlend Kristiansen N. G. Li A. I. Averensky A. E. Laugsand K. E. Zachariassen

Supercooling

Hardiness (plants)

Cold tolerance

Freezing tolerance

10.1007/s00360-009-0340-x

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Citations (8)

Inhibition of Gas Hydrate Nucleation and Growth: Efficacy of an Antifreeze Protein from the Longhorn Beetle Rhagium mordax

Energy & Fuels (2014)

Christine Malmos Perfeldt Pei Cheng Chua Nagu Daraboina Dennis Steven Friis Erlend Kristiansen

Antifreeze proteins (AFPs) are characterized by their ability to protect organisms from subfreezing temperatures by preventing tiny ice crystals in solution from growing as the solution is cooled below its freezing temperature. This inhibition of ice growth is called antifreeze activity, and in particular, certain insect AFPs show very high antifreeze activity. Recent studies have shown AFPs to be promising candidates as green and environmentally benign inhibitors for gas hydrate formation. Here we show that an insect antifreeze protein from the longhorn beetle, Rhagium mordax (RmAFP1), the most potent protein yet found for freezing inhibition, can inhibit methane hydrates as effectively as the synthetic polymeric inhibitor polyvinylpyrrolidone (PVP). In high pressure rocking cell experiments, onset hydrate nucleation temperatures and growth profiles showed repeatable results. RmAFP1 clearly showed inhibition of hydrates compared to amino acids (l-valine and l-threonine) and the protein bovine serum albumin (BSA). This indicates that proteins or amino acids do not generally inhibit hydrate formation. The promising performance of RmAFP1 as a new green kinetic hydrate inhibitor could further the development and increased production of green hydrate inhibitors.

Antifreeze protein

Clathrate hydrate

Antifreeze

Bovine serum albumin

Ice nucleus

10.1021/ef500349w

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Citations (94)

State-space representation of memory effects in foil lift force

IFAC Proceedings Volumes (2004)

Erlend Kristiansen Olav Egeland

Lift (data mining)