Related Experiment Video
Updated: Jul 30, 2026
Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System
Published on: September 16, 2011
An ice nucleation protein from Fusarium acuminatum: cloning, expression, biochemical characterization and
Milad Lagzian1, Ali Mohammad Latifi, Mohammad Reza Bassami
1Biotechnology Division, Faculty of Veterinary Medicine, Ferdowsi University of Mashhad, Mashhad, Iran, milad.lagzian@gmail.com.
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.
More Related Videos
08:46Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
Published on: January 15, 2014
09:43Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
