scholarly journals 1P110 Activity of recombinant antifreeze protein from basidiomycetes, Typhula ishikariensis

2005 ◽  
Vol 45 (supplement) ◽  
pp. S59
Author(s):  
K. Suzuki ◽  
M. Fujiwara ◽  
T. Hoshino ◽  
S. Ohgiya ◽  
S. Tsuda
Keyword(s):  
Antifreeze Protein ◽  
Typhula Ishikariensis

Antifreeze proteins from snow mold fungi

2003 ◽  
Vol 81 (12) ◽  
pp. 1175-1181 ◽  
Author(s):  
Tamotsu Hoshino ◽  
Michiko Kiriaki ◽  
Satoru Ohgiya ◽  
Mineko Fujiwara ◽  
Hidemasa Kondo ◽  
...  
Keyword(s):  
Extracellular Space ◽  
Antifreeze Proteins ◽  
Methylotrophic Yeast ◽  
Antifreeze Protein ◽  
Ice Crystals ◽  
Stone Age ◽  
Snow Mold ◽  
Typhula Ishikariensis ◽  
Hexagonal Ice ◽  
Molecular Masses

The psychrophilic fungi Coprinus psychromorbidus and Typhula ishikariensis produced unique antifreeze proteins (AFPs) in the extracellular space. Molecular masses of purified fungal AFPs of C. psychromorbidus and T. ishikariensis were approximately 22 and 23 kDa, respectively. Cloned genes of AFPs from T. ishikariensis do not have any similarity with known proteins. Purified fungal AFPs from cultural filtrate of T. ishikariensis and recombinant fungal AFP from methylotrophic yeast formed specific ice crystals resembling "Stone Age knives". These observations indicate that fungal AFPs do not form proper hexagonal ice crystals to inhibit their growth and that fungal AFPs can probably bind to surfaces of ice crystals in an irregular manner.Key words: antifreeze protein, snow mold fungi, Coprinus psychromorbidus, Typhula ishikariensis.

scholarly journals Ice Growth Suppression in the Solution Flows of Antifreeze Protein and Sodium Chloride in a Mini-Channel

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 306
Author(s):  
Kazuya Taira ◽  
Tomonori Waku ◽  
Yoshimichi Hagiwara
Keyword(s):  
Sodium Chloride ◽  
Synergistic Effects ◽  
Pure Water ◽  
Interface Velocity ◽  
Antifreeze Protein ◽  
Layer Growth ◽  
Mixed Solution ◽  
Solution Flow ◽  
Ice Growth ◽  
Cold Energy

The control of ice growth inside channels of aqueous solution flows is important in numerous fields, including (a) cold-energy transportation plants and (b) the preservation of supercooled human organs for transplantation. A promising method for this control is to add a substance that influences ice growth in the flows. However, limited results have been reported on the effects of such additives. Using a microscope, we measured the growth of ice from one sidewall toward the opposite sidewall of a mini-channel, where aqueous solutions of sodium chloride and antifreeze protein flowed. Our aim was to considerably suppress ice growth by mixing the two solutes. Inclined interfaces, the overlapping of serrated interfaces, and interfaces with sharp and flat tips were observed in the cases of the protein-solution, salt-solution, and mixed-solution flows, respectively. In addition, it was found that the average interface velocity in the case of the mixed-solution flow was the lowest and decreased by 64% compared with that of pure water. This significant suppression of the ice-layer growth can be attributed to the synergistic effects of the ions and antifreeze protein on the diffusion of protein.

scholarly journals Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
HaoQiang Yu ◽  
HongYing Zheng ◽  
Yuan Liu ◽  
QingQing Yang ◽  
WanChen Li ◽  
...  
Keyword(s):  
Temperature Stress ◽  
Heat Tolerance ◽  
Antifreeze Protein ◽  
Functional Domain ◽  
E Coli ◽  
Ammopiptanthus Nanus ◽  
Cold Sensitive ◽  
Crystal Binding ◽  
Function Expression ◽  
Response To Temperature

AbstractTemperature stress restricts plant growth and development. Antifreeze protein (AFP) can improve plants antifreeze ability. In our previous study, the AnAFP gene cloned from Ammopiptanthus nanus was confirmed to be an excellent candidate enhancing plant cold resistance. But, AnAFP protein shared similar structures with KnS type dehydrins including K, N and S domains except ice crystal binding domain A. Here, we generated AnAFPΔA, AnAFPΔK, AnAFPΔN and AnAFPΔS, and transformed them into ordinary and cold sensitive strains of E. coli, and Arabidopsis KS type dehydrin mutant to evaluate their function. Expression of AnAFPΔA decreases cold and heat tolerance in E. coli, meanwhile, AnAFP enhances heat tolerance in Arabidopsis, suggesting that domain A is a thermal stable functional domain. AnAFP, AnAFPΔA and AnAFPΔS localize in whole cell, but AnAFPΔK and AnAFPΔN only localizes in nucleus and cytoplasm, respectively, exhibiting that K and N domains control localization of AnAFP. Likewise, K domain blocks interaction between AnAFP and AnICE1. The result of RT-qPCR showed that expression of AnAFP, AnICE1 and AnCBF genes was significantly induced by high-temperature, indicating that the AnAFP is likely regulated by ICE1-CBF-COR signal pathway. Taken together, the study provides insights into understanding the mechanism of AnAFP in response to temperature stress and gene resource to improve heat or cold tolerance of plants in transgenic engineering.

scholarly journals Partial characterization of an antifreeze protein (CRY-c) from Cryobacterium psychrotolerans MLB-29 of Arctic glacier cryoconite

Polar Science ◽  
2021 ◽  
pp. 100661
Author(s):  
Purnima Singh ◽  
Sakae Tsuda ◽  
Shiv Mohan Singh ◽  
Sukanta Mondal ◽  
Utpal Roy
Keyword(s):  
Antifreeze Protein ◽  
Partial Characterization ◽  
Arctic Glacier

Induction of Winter Flounder Antifreeze Protein Messenger RNA at 4 C in vivo and in vitro

1986 ◽  
Vol 59 (6) ◽  
pp. 679-695 ◽  
Author(s):  
Jeffrey L. Price ◽  
Brian B. Gourlie ◽  
Yuan Lin ◽  
Ru Chih C. Huang
Keyword(s):  
Messenger Rna ◽  
Antifreeze Protein ◽  
Winter Flounder
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