• Bulletin of Food Technology
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• v.23 no.3
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• pp.376-384
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• 2010

• KSBB Journal
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• v.28 no.5
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• pp.310-314
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• 2013

Antifreeze peptide from Myoxocephalus octodecemspinosus was overexpressed and purified in Escherichia coli. Green fluorescence protein-AFP chimera was constructed by integrating gfp and afp genes. Produced GFP-AFP chimera protein was purified using polyhistidine tag which was inserted at C-terminus. By addition of GFP-AFP chimera protein, freezing point of elution buffer was decreased from $-13^{\circ}C$ to $-20^{\circ}C$. This result suggested that GFP-AFP chimera can be considered as a potential candidate of novel inhibitor for gas hydrates.

• Journal of the Korean Society of Manufacturing Process Engineers
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• v.15 no.5
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• pp.117-124
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• 2016

In this paper, we developed a breather valve with a water mist system for use near an oil storage tank. Our process applied a water mist system to the flame arrester to evaluate the fire suppression characteristics. For the fire suppression evaluation of the water mist system, we evaluated the angle of the nozzle, fire suppression, spray particle size, flashback, fire suppression time, and fire suppression test of antifreeze. Through the fire suppression test, the best fire suppression nozzle used an angle of $140^{\circ}$, and the flashback phenomenon of flame arrester did not occur. The fire suppression time of water mist system time was within three seconds, and the antifreeze was no problem with the fire suppression.

• Bulletin of the Korean Chemical Society
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• v.33 no.7
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• pp.2411-2414
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• 2012

• Korean Journal of Breeding Science
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• v.40 no.3
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• pp.234-242
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• 2008

To identify low temperature-induced genes of wheat chromosome substitution line 5D, suppression subtractive hybridization (SSH) was performed with mRNAs from leaf samples that treated with low temperature ($4^{\circ}C$). A cDNA library was constructed using mRNA isolated from wheat chromosome substitution line 5D leaves treated with low temperature ($4^{\circ}C$). The nucleotide and deduced amino acid sequences of the putative gene products were compared. wfr-9 and wfr-32 showed identity over 90% related to vernalization gene. Other two genes, wfr-77 and wfr-83 which is related to freezing-resistant gene have also identity over 90%. This result suggest that those genes may be transcribed into antifreeze proteins which are accumulated within leaf apoplasts, when wheat chromosome substitution line 5D is acclimated during low temperature treatment.

• Proceedings of the Korean Society of Crop Science Conference
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• 1998.04a
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• pp.195-196
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• 1998

• KSBB Journal
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• v.30 no.6
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• pp.345-349
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• 2015

Antifreeze proteins (AFP) inhibit growth and recrystallization of ice, and permit organisms to survive in cold environments. The AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris icebinding protein), was produced in E. coli using a cold shock induction system. The culture temperature was shifted from $37^{\circ}C$ to $15^{\circ}C$ and a 20 L culture scale was used. The final weights of dried cell and FfIBP were estimated to be 126 g and 8.4 g, respectively. The thermal hysteresis (TH) activity ($1.53^{\circ}C$) of the produced FfIBP was 3.6-fold higher than that of the LeIBP (Leucosporidium ice-binding protein) produced in Picha. The current study demonstrates that large-scale production of FfIBP was successful and the result could be extended to further application studies using recombinant AFPs.

• Korean Journal of Plant Tissue Culture
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• v.22 no.1
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• pp.15-28
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• 1995

In order to identify an antifreeze proteins responsible for freeze-tolerance in barley the proteins accumulated in extracellular space during cold acclimination were extracted and analyzed. After 42 days cold treatment there were several proteins sized of 70, 21, 16, 14 KDa increased in their amount accumulated in extracellular space. In addition, continuously sized polypeptides smaller than 10 KDa were found to be increased in their amount as cold treatment prolongs. Since these proteins were not detectable in total leaf protein extract it appears that the procedure used to isolate extracellular extract was valid. A similarity in profile of the extracellular proteins isolated from barley and rye may indicate a possibility for these proteins to be an antifreeze proteins since the same extract from rye was reported to show an antifreezing activity.

• Journal of Embryo Transfer
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• v.31 no.4
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• pp.355-365
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• 2016

The cryopreservation of sperm has become the subject of research for successful artificial insemination technologies. Antifreeze proteins (AFPs), one of the factors necessary for effective cryopreservation, are derived from certain Antarctic organisms. These proteins decrease the freezing point of water within these organisms to below the temperature of the surrounding seawater to protect the organism from cold shock. Accordingly, a recent study found that AFPs can increase the motility and viability of spermatozoa during cryopreservation. To evaluate this relationship, we performed cryopreservation of boar sperm with AFPs produced in the Arctic yeast Leucosporidium sp. AFP expression system at four concentrations (0, 0.01, 0.1, and $1{\mu}g/ml$) and evaluated motility using computer assisted sperm analysis. DNA damage to boar spermatozoa was measured by the comet assay, and sperm membrane integrity and acrosome integrity were evaluated by flow cytometry. The results showed that motility was positively affected by the addition of AFP at each concentration except $1{\mu}g/ml$ (p<0.001). Although cryopreservation with AFP decreased the viability of the boar sperm using, the tail DNA analyses showed that there was no significant difference between the control and the addition of 0.1 or $0.01{\mu}g/ml$ AFP. In addition, the percentage of live sperm with intact acrosomes showed the least significant difference between the control and $0.1{\mu}g/ml$ AFP (p<0.05), but increased with $1{\mu}g/ml$ AFP (p<0.001). Our results indicate that the addition of AFP during boar sperm cryopreservation can improve viability and acrosome integrity after thawing.

• KSBB Journal
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• v.29 no.4
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• pp.303-306
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• 2014

Antifreeze proteins (AFP) inhibit ice growth to permit the survival of polar organisms in the cold environments. The recombinant AFP from an Antarctic bacterium, Flavobacterium frigoris PS1, FfIBP (Flavobacterium frigoris ice-binding protein), was produced using Pichia pastoris expression system. The optimum fermentation temperature ($30^{\circ}C$) and pH (5) for FfIBP production were determined using a fed-batch culture system. The maximal cell density and purified FfIBP were 112 g/L and 70 mg/L, respectively. The thermal hysteresis (TH) activity (0.85) of FfIBP obtained using a glycerol-methanol fed-batch culture system was 2-fold higher than that of the LeIBP (Leucosporidium ice-binding protein). This work allows for large-scale production of FfIBP, which could be extended to further application studies using recombinant AFPs.