Malaysian Applied Biology Journal

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46_01_30

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Malays. Appl. Biol. (2017) 46(1): 213–218


CHARACTERIZATION AND POTENTIAL APPLICATIONS OF A

RECOMBINANT ANTIFREEZE PROTEIN FROM AN ANTARCTIC

YEAST Glaciozyma  antarctica  PRODUCED IN Pichia  pastoris

MD TAB, M.1, HASHIM, N.H.F.1, ABU BAKAR, F.D.1, ILLIAS, R.2, NAJIMUDIN, N.3,

MAHADI, N.M.4 and MURAD, A.M.A.1*

1School of Biosciences and Biotechnology, Faculty of Science and Technology,
Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, Malaysia
2Department of Bioprocess Engineering, Faculty of Chemical and Natural Resources Engineering,
Universiti Teknologi Malaysia, 81310 Skudai, Johor, Malaysia
3School of Biological Sciences, Universiti Sains Malaysia, 11800 Penang, Malaysia
4Malaysia Genome Institute, Jalan Bangi Lama, 43000 Kajang, Selangor, Malaysia

*Email: This e-mail address is being protected from spambots. You need JavaScript enabled to view it

Accepted 2 February 2017, Published online 31 March 2017

 

ABSTRACT

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 sub-zero 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.

Key words: antifreeze protein, Glaciozyma antarctica, recrystallization inhibition, cryoprotective

 

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