title: An ice nucleation protein from Fusarium acuminatum: cloning, expression, biochemical characterization and computational modeling.
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.
authors.affiliation: Biotechnology Division, Faculty of Veterinary Medicine, Ferdowsi University of Mashhad, Mashhad, Iran, milad.lagzian@gmail.com.
authors.forename: Milad
authors.initials: M
authors.lastname: Lagzian
authors.forename: Ali Mohammad
authors.initials: AM
authors.lastname: Latifi
authors.forename: Mohammad Reza
authors.initials: MR
authors.lastname: Bassami
authors.forename: Morteza
authors.initials: M
authors.lastname: Mirzaei
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005670:Fusarium / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D001425:Bacterial Outer Membrane Proteins; D005656:Fungal Proteins; C063113:ice nucleation protein