Antifreeze Glycoproteins—Preventing the Growth of Ice

Ben, Robert N.

doi:10.1002/1439-7633(20010302)2:3<161::aid-cbic161>3.0.co;2-f

Cited by 66 publications

(59 citation statements)

References 80 publications

(20 reference statements)

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“…[55][56][57] For example, antifreeze glycoproteins (AFGPs) isolated from fish blood plasma consist of a regular tripeptide sequence of Ala-Ala-Thr with a disaccharide fragment (-D-galactosyl-(1-3)--D-galactosamine) linked to the threonine residue. [58][59][60][61] It is noteworthy that the polysaccharide described here displays a structural feature very close to that present in AFGPs. Actually, a -N-acetyl-galactosamine is substituted by an -galacturonosyl residue bearing an amide-linked threonine.…”

Section: Discussionsupporting

confidence: 53%

A Unique Capsular Polysaccharide Structure from the Psychrophilic Marine Bacterium Colwellia psychrerythraea 34H That Mimics Antifreeze (Glyco)proteins

et al. 2015

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ABSTRACT:The low temperatures of polar regions and high altitude environments, especially icy habitats, present challenges for many microorganisms. Their ability to live under subfreezing conditions implies the production of compounds conferring cryotolerance. Colwellia psychrerythraea 34H, a -proteobacterium isolated from subzero Arctic marine sediments, provides a model for the study of life in cold environments. We report here the identification and detailed molecular primary and secondary structures of capsular polysaccharide from C. psychrerythraea 34H cells. The polymer was isolated in the water layer when cells were extracted by phenol/water and characterized by one-and two-dimensional NMR spectroscopy together with chemical analysis. Molecular mechanic and dynamic calculations were also performed. The polysaccharide consists of a tetrasaccharidic repeating unit containing two amino sugars and two uronic acids bearing threonine as substituent. The structural features of this unique polysaccharide resemble those present in antifreeze proteins and glycoproteins. These results suggest a possible correlation between the capsule structure and the ability of C. psychrerythraea to colonize subfreezing marine environments.

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Section: Discussionsupporting

confidence: 53%

A Unique Capsular Polysaccharide Structure from the Psychrophilic Marine Bacterium Colwellia psychrerythraea 34H That Mimics Antifreeze (Glyco)proteins

et al. 2015

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“…[21], Flavobacterium frigoris [7], Glaciozyma antarctica [12,22], Navicula glaciei [16], Fragilariopsis cylindrus [23,24], and Chaetocero neoglacile [15]. The unique function of AFPs, i.e., enabling fish to survive in subfreezing environments, has inspired the researchers in academia and industries to examine the potential applications of AFPs as a potential cryoprotective agents or cryoprotectants (CPAs) in the cryopreservation of biological samples [25,26,27,28,29,30,31]. In this review, we discuss the biophysical and biochemical aspects of marine-derived AFPs as well as investigate past and current research of the practical applications of AFPs in cryopreservation.…”

Section: Introductionmentioning

confidence: 99%

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

et al. 2017

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Antifreeze proteins (AFPs) are biological antifreezes with unique properties, including thermal hysteresis (TH), ice recrystallization inhibition (IRI), and interaction with membranes and/or membrane proteins. These properties have been utilized in the preservation of biological samples at low temperatures. Here, we review the structure and function of marine-derived AFPs, including moderately active fish AFPs and hyperactive polar AFPs. We also survey previous and current reports of cryopreservation using AFPs. Cryopreserved biological samples are relatively diverse ranging from diatoms and reproductive cells to embryos and organs. Cryopreserved biological samples mainly originate from mammals. Most cryopreservation trials using marine-derived AFPs have demonstrated that addition of AFPs can improve post-thaw viability regardless of freezing method (slow-freezing or vitrification), storage temperature, and types of biological sample type.

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“…얼음결정의 성장을 억제 하는 특성은 냉동보관, 음식물 보존, 유전자변형 기술, 냉동 수술 분야 등에 이용될 수 있어 결빙방지단백질은 학계와 산 업계의 관심을 끌고 있다 [3][4][5][6][7]. 자연계로부터 결빙방지단백 질을 획득하는 것은 자원이 제한되고 경제성도 낮아 실현하 기 어려워 이종발현을 이용하여 생산하는 연구가 진행되고 있다.…”

Section: Introductionunclassified

Pilot-scale Production of the Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by Recombinant Escherichia coli with a Cold Shock Induction System

Kim¹,

Lee²,

Lee³

et al. 2015

KSBB Journal

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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°C to 15°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°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.

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Antifreeze Glycoproteins—Preventing the Growth of Ice

Cited by 66 publications

References 80 publications

A Unique Capsular Polysaccharide Structure from the Psychrophilic Marine Bacterium Colwellia psychrerythraea 34H That Mimics Antifreeze (Glyco)proteins

A Unique Capsular Polysaccharide Structure from the Psychrophilic Marine Bacterium Colwellia psychrerythraea 34H That Mimics Antifreeze (Glyco)proteins

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

Pilot-scale Production of the Antifreeze Protein from Antarctic Bacterium Flavobacterium frigoris PS1 by Recombinant Escherichia coli with a Cold Shock Induction System

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