Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris
Ice recrystallization during thawing post-cryopreservation results in extensive cellular damage and ultimately leads to cell death and reduced cell viability. Antifreeze proteins (AFPs) are a group of proteins that allow organisms to survive in subzero environments. These proteins have thermal hyste...
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Malaysian Society of Applied Biology
2017
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| author | Md. Tab, M. Hashim, N. H. F. Abu Bakar, F. D. Illias, R. Najimudin, N. Mahadi, N. M. Murad, A. M. A. |
| author_facet | Md. Tab, M. Hashim, N. H. F. Abu Bakar, F. D. Illias, R. Najimudin, N. Mahadi, N. M. Murad, A. M. A. |
| author_sort | Md. Tab, M. |
| collection | ePrints |
| description | Ice recrystallization during thawing post-cryopreservation results in extensive cellular damage and ultimately leads to cell death and reduced cell viability. Antifreeze proteins (AFPs) are a group of proteins that allow organisms to survive in subzero environments. These proteins have thermal hysteresis and ice recrystallization inhibitory activities. In this present study, we demonstrated the efficiency of a recombinant antifreeze protein from the Antarctic yeast, Glaciozyma antarctica, as a recrystallization inhibitor (RI) of ice growth and assessed its application as a cryopreservative of the fungal cutinase enzyme against freeze-thaw cycles. Recombinant Afp1 from G. antarctica, a psychrophilic yeast, has been produced in a methylotrophic yeast, Pichia pastoris, system that results in the expression of a hyper-glycoprotein (~55 kDa). Recombinant Afp1 exhibits antifreeze functions: thermal hysteresis (TH) and recrystallization inhibition where the highest TH values recorded for ~0.5°C at 10 mg/mL. The cryoprotective effects of Afp1 on purified recombinant cutinase showed that Afp1 can retain enzymatic activity up to ~20% when subjected to several cycles of freeze thawing. These findings indicate that Afp1 might act as a cryoprotective agent and thus, has great potential in biotechnology applications. |
| first_indexed | 2024-03-05T20:13:39Z |
| format | Article |
| id | utm.eprints-76795 |
| institution | Universiti Teknologi Malaysia - ePrints |
| last_indexed | 2024-03-05T20:13:39Z |
| publishDate | 2017 |
| publisher | Malaysian Society of Applied Biology |
| record_format | dspace |
| spelling | utm.eprints-767952018-04-30T14:07:34Z http://eprints.utm.my/76795/ Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris Md. Tab, M. Hashim, N. H. F. Abu Bakar, F. D. Illias, R. Najimudin, N. Mahadi, N. M. Murad, A. M. A. TP Chemical technology Ice recrystallization during thawing post-cryopreservation results in extensive cellular damage and ultimately leads to cell death and reduced cell viability. Antifreeze proteins (AFPs) are a group of proteins that allow organisms to survive in subzero environments. These proteins have thermal hysteresis and ice recrystallization inhibitory activities. In this present study, we demonstrated the efficiency of a recombinant antifreeze protein from the Antarctic yeast, Glaciozyma antarctica, as a recrystallization inhibitor (RI) of ice growth and assessed its application as a cryopreservative of the fungal cutinase enzyme against freeze-thaw cycles. Recombinant Afp1 from G. antarctica, a psychrophilic yeast, has been produced in a methylotrophic yeast, Pichia pastoris, system that results in the expression of a hyper-glycoprotein (~55 kDa). Recombinant Afp1 exhibits antifreeze functions: thermal hysteresis (TH) and recrystallization inhibition where the highest TH values recorded for ~0.5°C at 10 mg/mL. The cryoprotective effects of Afp1 on purified recombinant cutinase showed that Afp1 can retain enzymatic activity up to ~20% when subjected to several cycles of freeze thawing. These findings indicate that Afp1 might act as a cryoprotective agent and thus, has great potential in biotechnology applications. Malaysian Society of Applied Biology 2017 Article PeerReviewed Md. Tab, M. and Hashim, N. H. F. and Abu Bakar, F. D. and Illias, R. and Najimudin, N. and Mahadi, N. M. and Murad, A. M. A. (2017) Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris. Malaysian Applied Biology, 46 (1). pp. 213-218. ISSN 0126-8643 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017157880&partnerID=40&md5=a878e949064b9bf0d63b069c0cc4acb1 |
| spellingShingle | TP Chemical technology Md. Tab, M. Hashim, N. H. F. Abu Bakar, F. D. Illias, R. Najimudin, N. Mahadi, N. M. Murad, A. M. A. Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title | Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title_full | Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title_fullStr | Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title_full_unstemmed | Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title_short | Characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast Glaciozyma antarctica produced in Pichia pastoris |
| title_sort | characterization and potential applications of a recombinant antifreeze protein from an antarctic yeast glaciozyma antarctica produced in pichia pastoris |
| topic | TP Chemical technology |
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