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Optimization of the pilot-scale production of an ice-binding protein by fed-batch culture of Pichia pastoris

Cited 23 time in wos
Cited 28 time in scopus

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dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Hak Jun-
dc.contributor.authorHan, Se Jong-
dc.contributor.authorYong-Hoe Choe-
dc.contributor.authorEunjung Kim-
dc.contributor.authorJong Chan Park-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorLee, Sung Gu-
dc.date.accessioned2018-03-20T13:42:12Z-
dc.date.available2018-03-20T13:42:12Z-
dc.date.issued2013-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/6137-
dc.description.abstractIce-binding proteins (IBPs) can bind to the ice crystal and inhibit its growth. Because this property of IBPs can increase the freeze-thaw survival of cells, IBPs has attracted the attention from industries for their potential use in biotechnoogical applications. However, their use was largely hampered by the lack of the large-scale recombinant production system. In this study, the codon-optimized IBP from Leucosporidium sp. (LeIBP) was constructed and subjected to high-level expression in methylotrophic Pichia pastoris sytem. In a laboratory-scale fermentation (7 L), the optimal induction temperature and pH were determined to be 25°C and 6.0, respectively. Further, employing glycerol fed-batch phase prior to methanol induction phase enhanced the production of recombinant LelBP (rLeIBP) by ~100 mg/L. The total amount of secreted proteins at these conditions (25°C, pH 6.0, and glycerol fed-batch phase) was ~443 mg/L, 60 % of which was rLeIBP, yielding ~272 mg/L. In the pilot scale fermentation (700 L) under the same conditions, the yield of rLeIBP was 300 mg/L. To our best knowledge, this result reports the highest production yield of the recombinant IBP. More importantly, the rLeIBP secreted into culture media was stable and active for six days of fermentation. The thermal hysteresis (TH) activity of rLeIBP was about 0.42°C, which is almost the same to those reported previously. The avaotechnoogical applications. However, their use was largely hampered by the lack of the large-scale recombinant production system. In this study, the codon-optimized IBP from Leucosporidium sp. (LeIBP) was constructed and subjected to high-level expression in methylotrophic Pichia pastoris sytem. In a laboratory-scale fermentation (7 L), the optimal induction temperature and pH were determined to be 25°C and 6.0, respectively. Further, employing glycerol fed-batch phase prior to methanol induction phase enhanced the production of recombinant LelBP (rLeIBP) by ~100 mg/L. The total amount of secreted proteins at these conditions (25°C, pH 6.0, and glycerol fed-batch phase) was ~443 mg/L, 60 % of which was rLeIBP, yielding ~272 mg/L. In the pilot scale fermentation (700 L) under the same conditions, the yield of rLeIBP was 300 mg/L. To our best knowledge, this result reports the highest production yield of the recombinant IBP. More importantly, the rLeIBP secreted into culture media was stable and active for six days of fermentation. The thermal hysteresis (TH) activity of rLeIBP was about 0.42°C, which is almost the same to those reported previously. The ava-
dc.languageEnglish-
dc.publisherSpringer-
dc.subjectBiotechnology & Applied Microbiology-
dc.titleOptimization of the pilot-scale production of an ice-binding protein by fed-batch culture of Pichia pastoris-
dc.title.alternative피키아 발현시스템을 이용한 LeIBP 결빙방지단백질의 대량생산 최적화 연구 (공동 제1저자)-
dc.typeArticle-
dc.identifier.bibliographicCitationLee, Jun Hyuck, et al. 2013. "Optimization of the pilot-scale production of an ice-binding protein by fed-batch culture of Pichia pastoris". <em>APPLIED MICROBIOLOGY AND BIOTECHNOLOGY</em>, 97(8): 3383-3393.-
dc.citation.titleAPPLIED MICROBIOLOGY AND BIOTECHNOLOGY-
dc.citation.volume97-
dc.citation.number8-
dc.identifier.doi10.1007/s00253-012-4594-y-
dc.citation.startPage3383-
dc.citation.endPage3393-
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2011:24.68-
dc.subject.keywordFed-batch culture-
dc.subject.keywordIce-binding protein-
dc.subject.keywordLeIBP-
dc.subject.keywordLeucosporidium sp.-
dc.subject.keywordPichia pastoris-
dc.identifier.localId2013-0198-
dc.identifier.scopusid2-s2.0-84876675282-
dc.identifier.wosid000317136700013-
Appears in Collections  
2011-2012, Developing cryoprotectant materials derived from antifreeze proteins for the cryopreservation of valuable bioresources (11-12) / Kim, Hak Jun (PE11100, PG11010, PG12010, PE12210)
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