Abstract
Ice nucleation proteins (INP) are a major cause of frost damage in plants and crops. Here, an INP gene from Fusarium acuminatum was optimized, synthesized, expressed in E.coli and subsequently purified and characterized. The protein belongs to the second class of ice nucleation proteins with an optimum pH 5.5, relative activity and stability between pH 5 and 9.5 and up to 45 °C. The protein was fully active and stable in the presence of dimethyl sulfoxide (DMSO), dioxane, acetone and ethyl acetate. Moreover, it retained over 50 % of its original activity in the presence of polyvinyl alcohol. The 3D structure model of the INP-F indicated the protein had three distinct domains as exist in other ice nucleation proteins with some variations. Considering these promising results, INP-F could be a novel candidate for industrial applications.
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Acknowledgments
We greatly appreciate the Biotechnology Division members of Ferdowsi University of Mashhad for their help. We especially thank Dr. Hakimeh Ebrahimi Nik for critical review of the manuscript. This work was supported by grants from Baqiyatallah University of Medical Sciences, which is gratefully acknowledged by the authors.
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Lagzian, M., Latifi, A.M., Bassami, M.R. et al. An ice nucleation protein from Fusarium acuminatum: cloning, expression, biochemical characterization and computational modeling. Biotechnol Lett 36, 2043–2051 (2014). https://doi.org/10.1007/s10529-014-1568-4
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DOI: https://doi.org/10.1007/s10529-014-1568-4