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Protection of Alcohol Dehydrogenase against Freeze-Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property

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dc.contributor.authorLee, Young Hoon-
dc.contributor.authorKim, Kitae-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Hak Jun-
dc.date.accessioned2021-04-30T07:27:52Z-
dc.date.available2021-04-30T07:27:52Z-
dc.date.issued2020-12-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/11794-
dc.description.abstractIce-binding proteins (IBPs) have ice recrystallization inhibition (IRI) activity. IRI property has been extensively utilized for the cryopreservation of different types of cells and tissues. Recent reports demonstrated that IRI can also play a significant role in protecting proteins from freezing damage during freeze-thaw cycles. In this study, we hypothesized that the protective capability of IBPs on proteins against freeze-thaw damage is proportional to their IRI activity. Hence we used two IBPs: one with higher IRI activity (LeIBP) and the other with lower activity (FfIBP). Yeast alcohol dehydrogenase (ADH) was used as a freeze-labile model protein. IBPs and ADH were mixed, frozen at -20 degrees C, and thawed repeatedly. The structure of ADH was assessed using fluorescence emission spectra probed by 1-anilinonaphthalene-8-sulfonate over the repeated freeze-thaw cycles. The activity was monitored at 340 nm spectrophotometrically. Fluorescence data and activity clearly indicated that ADH without IBP was freeze-labile. However, ADH maintained about 70% residual activity after five repeated cycles at a minimal concentration of 0.1 mg mL(-1) of high IRI-active LeIBP, but only 50% activity at 4 mg mL(-1) of low active FfIBP. These results showed that the protection of proteins from freeze-thaw stress by IBPs is proportional to their IRI activity.en_US
dc.languageEnglishen_US
dc.language.isoen_USen_US
dc.subjectPharmacology & Pharmacyen_US
dc.subject.classificationDasan Stationen_US
dc.titleProtection of Alcohol Dehydrogenase against Freeze-Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Propertyen_US
dc.title.alternativeAlcohol Dehydrogenase 효소의 냉동 보관을 위해 결빙방지단백질을 사용 할 때 얼음 재결정화 억제활성이 중요하다는 사실 규명en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationLee, Young Hoon, et al. 2020. "Protection of Alcohol Dehydrogenase against Freeze-Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property". <em>MARINE DRUGS</em>, 18(12): 638-648.en_US
dc.citation.titleMARINE DRUGSen_US
dc.citation.volume18en_US
dc.citation.number12en_US
dc.identifier.doi10.3390/md18120638-
dc.citation.startPage638en_US
dc.citation.endPage648en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2018:24.59en_US
dc.subject.keywordice-binding proteinen_US
dc.subject.keywordice recrystallization inhibitionen_US
dc.subject.keywordalcohol dehydrogenaseen_US
dc.subject.keywordantifreeze proteinen_US
dc.subject.keywordfreezing damageen_US
dc.identifier.localId2020-0260-
dc.identifier.scopusid2-s2.0-85098533719-
dc.identifier.wosid000602722000001-
Appears in Collections  
2020-2020, Investigation of ice microstructure properties for developing low-temperature purification and environment/energy materials (20-20) / Kim, Kitae (PE20030)
2020-2020, Development of potential candidates as antibiotics based on polar genetic resources (20-20) / Lee, Jun Hyuck (PM20030)
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