Online citations, reference lists, and bibliographies.
← Back to Search

Characterization Of Afp1, An Antifreeze Protein From The Psychrophilic Yeast Glaciozymaantarctica PI12

N. Hashim, I. Bharudin, Douglas Law Sie Nguong, Sakura Higa, F. Bakar, S. Nathan, A. Rabu, H. Kawahara, R. Illias, N. Najimudin, N. Mahadi, Abdul Munir Abdul Murad
Published 2012 · Biology, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy Visualize in Litmaps
Share
Reduce the time it takes to create your bibliography by a factor of 10 by using the world’s favourite reference manager
Time to take this seriously.
Get Citationsy
The psychrophilic yeast Glaciozyma antarctica demonstrated high antifreeze activity in its culture filtrate. The culture filtrate exhibited both thermal hysteresis (TH) and ice recrystallization inhibition (RI) properties. The TH of 0.1 °C was comparable to that previously reported for bacteria and fungi. A genome sequence survey of the G. antarctica genome identified a novel antifreeze protein gene. The cDNA encoded a 177 amino acid protein with 30 % similarity to a fungal antifreeze protein from Typhula ishikariensis. The expression levels of AFP1 were quantified via real time-quantitative polymerase chain reaction (RT-qPCR), and the highest expression levels were detected within 6 h of growth at −12 °C. The cDNA of the antifreeze protein was cloned into an Escherichia coli expression system. Expression of recombinant Afp1 in E. coli resulted in the formation of inclusion bodies that were subsequently denatured by treatment with urea and allowed to refold in vitro. Activity assays of the recombinant Afp1 confirmed the antifreeze protein properties with a high TH value of 0.08 °C.
This paper references
10.1016/s0021-9258(18)63073-x
Chemical and physical properties of freezing point-depressing glycoproteins from Antarctic fishes.
A. Devries (1970)
Cleavage of structural proteins during
U. K. Laemmli (1970)
10.1016/s0140-6736(59)91597-1
Psychrophilic bacteria.
R. Morita (1975)
10.1016/0003-2697(76)90527-3
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
M. M. Bradford (1976)
10.1093/NAR/8.19.4321
Rapid isolation of high molecular weight plant DNA.
M. Murray (1980)
RAPID ISOLATION OF HIGH-MOLECULAR WEIGHT DNA
M. G. Murray (1980)
10.1016/0076-6879(86)27024-X
Antifreeze glycopeptides and peptides: interactions with ice and water.
A. Devries (1986)
10.1073/PNAS.87.23.9265
An antifreeze glycopeptide gene from the antarctic cod Notothenia coriiceps neglecta encodes a polyprotein of high peptide copy number.
K. C. Hsiao (1990)
10.1111/J.1432-1033.1992.TB19824.X
Protein interaction with ice.
C. Hew (1992)
10.1016/S0006-3495(93)81361-4
Adsorption to ice of fish antifreeze glycopeptides 7 and 8.
C. Knight (1993)
Adsorption to ice of fish
CA Knight (1993)
10.1073/PNAS.93.13.6835
Antifreeze glycoproteins inhibit leakage from liposomes during thermotropic phase transitions.
L. M. Hays (1996)
Effects of antifreeze proteins on red blood cell survival during cryopreservation.
H. Chao (1996)
10.1038/41908
Hyperactive antifreeze protein from beetles
L. Graham (1997)
10.1139/W97-126
Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
H. Xu (1998)
10.1385/1-59259-584-7:531
Protein identification and analysis tools in the ExPASy server.
M. Wilkins (1999)
10.1104/PP.119.4.1361
Antifreeze proteins in winter rye leaves form oligomeric complexes
Yu (1999)
10.1016/S0014-5793(99)01588-4
New ice‐binding face for type I antifreeze protein
J. Baardsnes (1999)
10.1007/s000180050289
Structure, function and evolution of antifreeze proteins
K. Ewart (1999)
10.1021/BI990613S
A complex family of highly heterogeneous and internally repetitive hyperactive antifreeze proteins from the beetle Tenebrio molitor.
Y. Liou (1999)
10.1094/PHYTO.2000.90.4.354
Role of ice nucleation and antifreeze activities in pathogenesis and growth of snow molds.
C. Snider (2000)
10.1016/S1357-2725(00)00083-2
Thermal hysteresis proteins.
J. Barrett (2001)
10.1006/CRYO.2001.2321
Flounder antifreeze peptides increase the efficacy of cryosurgery.
K. Muldrew (2001)
10.1146/ANNUREV.PHYSIOL.63.1.359
Antifreeze proteins of teleost fishes.
G. Fletcher (2001)
10.1016/S0006-3495(01)75986-3
A theoretical model of a plant antifreeze protein from Lolium perenne.
M. J. Kuiper (2001)
10.2210/PDB1I3B/PDB
THEORETICAL BETA-HELIX MODEL OF A PLANT ANTIFREEZE PROTEIN FROM LOLIUM PERENNE.
M. J. Kuiper (2001)
Flounder antifreeze
M Olson (2001)
10.1046/J.0014-2956.2001.02628.X
A family of expressed antifreeze protein genes from the moth, Choristoneura fumiferana.
D. Doucet (2002)
10.1016/S0968-0004(01)02028-X
Antifreeze proteins: an unusual receptor-ligand interaction.
Z. Jia (2002)
10.1016/S0260-8774(01)00209-6
Novel methods for rapid freezing and thawing of foods - a review
Bing Li (2002)
Antifreeze proteins: an unusual receptor
Z Jia (2002)
10.1016/S1010-7940(03)00306-3
Preservation of myocyte structure and mitochondrial integrity in subzero cryopreservation of mammalian hearts for transplantation using antifreeze proteins--an electron microscopy study.
G. Amir (2003)
10.1139/B03-116
Antifreeze proteins from snow mold fungi
T. Hoshino (2003)
Antifreeze proteins from snow mold
I Yumoto (2003)
10.1016/J.TPLANTS.2004.06.007
Antifreeze proteins in overwintering plants: a tale of two activities.
M. Griffith (2004)
Cloning and Expression of afpA , a Gene Encoding an Antifreeze Protein from the Arctic Plant Growth-Promoting Rhizobacterium Pseudomonas putida GR 12-2 †
N. Muryoi (2004)
10.1128/JB.186.17.5661-5671.2004
Cloning and expression of afpA, a gene encoding an antifreeze protein from the arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2.
N. Muryoi (2004)
Reduction of freeze-thaw-induced hemolysis of red blood cells by an algal ice-binding protein.
Jae-Shin Kang (2004)
10.1016/J.JMB.2004.05.028
Improved prediction of signal peptides: SignalP 3.0.
J. D. Bendtsen (2004)
10.1007/BF00262308
Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis
D. W. Wu (2004)
Cloning and expression of afpA
M Griffith (2004)
Reduction of freeze-thaw-induced
K Jae-Shin (2004)
10.1529/BIOPHYSJ.104.056770
Why does insect antifreeze protein from Tenebrio molitor produce pyramidal ice crystallites?
C. S. Strom (2005)
10.1110/ps.041009005
Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli
Susan Idicula-Thomas (2005)
10.1093/PROTEIN/GZI022
Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation.
Susan Idicula-Thomas (2005)
10.1016/J.FEMSLE.2005.02.022
A hyperactive, Ca2+-dependent antifreeze protein in an Antarctic bacterium.
J. Gilbert (2005)
Protein identification and analysis tools on the ExPASy server A hyperactive, Ca 2? dependent antifreeze protein in an Antarctic bacterium
E Gasteiger (2005)
10.1038/sj.embor.7400662
Psychrophilic microorganisms: challenges for life
S. D’Amico (2006)
10.3168/JDS.S0022-0302(06)72068-9
Ice recrystallization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass.
A. Regand (2006)
10.1038/nbt1224
Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions
A. C. Doxey (2006)
10.1016/J.FOODRES.2007.01.006
Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough
Chao Zhang (2007)
A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum.
H. Kawahara (2007)
10.1111/J.1574-6941.2007.00345.X
An ice-binding protein from an Antarctic sea ice bacterium.
J. Raymond (2007)
An ice-binding protein
JA Raymond (2007)
A novel, intracellular antifreeze
H Omura (2007)
10.1128/AEM.02000-07
Coping with Our Cold Planet
D. F. Rodrigues (2008)
10.1080/07388550801891152
Properties, potentials, and prospects of antifreeze proteins.
S. Venketesh (2008)
10.1373/clinchem.2008.112797
The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments.
S. Bustin (2009)
10.1111/j.1742-4658.2009.07490.x
Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis
Nan Xiao (2010)
10.1016/j.cryobiol.2010.01.002
An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast.
J. Lee (2010)
Molecular cloning , expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI 12
A. Ramli (2011)
10.1186/1475-2859-10-94
Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12
A. M. Ramli (2011)
10.1074/jbc.M111.331835
Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast*
J. Lee (2012)
10.1073/pnas.1121607109
Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation
H. Kondo (2012)
Extremophiles
(2013)
We acknowledge support given by the Australian Antarctic Division and the Malaysian Antarctic Research Programme (MARP) of the Academy of Science
Ukm-Mgi Grants



This paper is referenced by
10.3390/jof7070528
Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast, Glaciozyma antarctica PI12
N. A. Yusof (2021)
10.26502/IJABPT.202101
The Cold-Active Endo-β-1,3(4)-Glucanase from a Marine Psychrophilic Yeast, Glaciozyma antarctica PI12: Heterologous Expression, Biochemical Characterisation, and Molecular Modeling
Salimeh Mohammadi (2021)
10.1016/j.bcab.2019.101447
Rational design of short antifreeze peptides derived from Rhagium inquisitor antifreeze protein
Lai Fun Kong (2020)
10.1007/978-3-030-41929-5_8
Antifreeze Proteins in Other Species
J. G. Duman (2020)
10.12691/AJMR-8-2-4
Lactic Acid Bacteria and Yeasts in Spontaneously Fermented Sorghum Sourdough
Motunrayo O. Ewuoso (2020)
10.1016/j.theriogenology.2020.04.016
The protective effect of Leucosporidium-derived ice-binding protein (LeIBP) on bovine oocytes and embryos during vitrification.
Wu-Sheng Sun (2020)
10.1007/978-3-030-41929-5
Antifreeze Proteins Volume 1: Environment, Systematics and Evolution
H. Ramløv (2020)
10.13679/J.ADVPS.2019.0030
Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica
J. Charles (2020)
10.3390/biom10020274
Ice Binding Proteins: Diverse Biological Roles and Applications in Different Types of Industry
A. Białkowska (2020)
10.5614/crbb.2020.2.1/tlcy1641
Phenazine-1-carboxylic acid (PCA) from Cold-Adapted Yeast Glaciozyma antarctica PI12
Andi Rifki Rosandy (2020)
10.1038/s41467-020-16073-3
Stress-induced expression is enriched for evolutionarily young genes in diverse budding yeasts
Tyler W. Doughty (2020)
10.1893/BIOS-D-17-00007
Antifreeze proteins: effective adaptations of organisms for low temperature survival
Steven Bagwell (2019)
10.1016/j.ijbiomac.2019.12.099
Functional and structural analyses of an expansin-like protein from the antarctic yeast Glaciozyma antarctica PI12 reveal strategies of nutrient scavenging in the sea ice environment.
Nooraisyah Mohamad Nor (2019)
10.3390/biom9050181
The Use of Antifreeze Proteins in the Cryopreservation of Gametes and Embryos
V. Robles (2019)
10.1007/s12192-019-00969-1
Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica
Nur Athirah Yusof (2019)
10.3389/fmicb.2019.00557
Darkening of the Greenland Ice Sheet: Fungal Abundance and Diversity Are Associated With Algal Bloom
Laura Perini (2019)
10.1016/J.POLAR.2018.11.007
Gene expression patterns of Glaciozyma antarctica PI12 in response to cold, and freeze stress
J. S. P. Koh (2019)
10.1101/660274
Stress-Induced Expression is Enriched for Evolutionarily Young Genes in Diverse Budding Yeasts
Tyler W. Doughty (2019)
10.1371/journal.pone.0189947
The Glaciozyma antarctica genome reveals an array of systems that provide sustained responses towards temperature variations in a persistently cold habitat
Mohd Firdaus-Raih (2018)
10.17576/JSM-2018-4711-12
(-)-glaciantarcin, a new dipeptide and some secondary metabolites from the psychrophilic yeast Glaciozyma antarctica PI12
Andi Rifki Rosandy (2018)
10.1007/s00792-018-1015-x
Draft genome sequences of bacteria isolated from the Deschampsia antarctica phyllosphere
Fernanda P. Cid (2018)
10.1186/s12866-018-1214-8
Antarctic yeasts: analysis of their freeze-thaw tolerance and production of antifreeze proteins, fatty acids and ergosterol
P. Villarreal (2018)
10.1039/c8cp04727h
Multiple binding modes of a moderate ice-binding protein from a polar microalga.
H. Kondo (2018)
10.1073/pnas.1807461115
Growth suppression of ice crystal basal face in the presence of a moderate ice-binding protein does not confer hyperactivity
M. Bayer-Giraldi (2018)
10.1016/j.marenvres.2018.03.007
Unravelling the adaptation strategies employed by Glaciozyma antarctica PI12 on Antarctic sea ice.
I. Bharudin (2018)
10.1039/c8cc05588b
Design and synthesis of galactose-conjugated fluorinated and non-fluorinated proline oligomers: towards antifreeze molecules.
Y. Sumii (2018)
10.1007/S13369-017-2738-1
Large-Scale Production of Glaciozyma antarctica Antifreeze Protein 1 (Afp1) by Fed-Batch Fermentation of Pichia pastoris
M. M. Tab (2018)
10.1007/s00792-018-1021-z
Biochemical and structural characterization of a novel cold-active esterase-like protein from the psychrophilic yeast Glaciozyma antarctica
Noor Haza Fazlin Hashim (2018)
10.1186/s12859-018-2550-2
Computational discovery and annotation of conserved small open reading frames in fungal genomes
Shuhaila Mat-Sharani (2018)
Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris
M. M. Tab (2017)
10.3390/md15020027
Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant
H. J. Kim (2017)
10.17576/MJAS-2017-2106-05
Diketopiperazin dihasilkan oleh yis psikropilik Glaciozyma antarctica PI12
Andi Rifki Rosandy (2017)
See more
Semantic Scholar Logo Some data provided by SemanticScholar