TAILIEUCHUNG - Báo cáo khoa học: Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis

Antifreeze proteins are structurally diverse polypeptides that have thermal hysteresis activity and have been discovered in many cold-adapted organ-isms. Of these, fungal antifreeze protein has been purified and partially characterized only in a species of psychrophilic basidiomycete, Typhula ishikariensis. | Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis Nan Xiao1 2 Keita Suzuki1 2 Yoshiyuki Nishimiya1 Hidemasa Kondo1 Ai Miura1 Sakae Tsuda1 2 and Tamotsu Hoshino1 2 1 Research Institute of Genome-based Biofactory National institute of Advanced Industrial science and Technology AIST Toyohira-ku Sapporo Japan 2 Division of BiologicalSciences Graduate Schoolof Science Hokkaido University Kita-ku Sapporo Japan Keywords fungalAFP ice growth inhibition psychrophile recrystallization inhibition thermal hysteresis Correspondence S. Tsuda FunctionalProtein Research Group Research Institute of Genome-Based Biofactory NationalInstitute of Advanced IndustrialScience and Technology AIST 2-17-2-1 Tsukisamu-Higashi Toyohira-ku Sapporo 062-8517 Japan Fax 81 11 857 8983 Tel 81 11 857 8983 E-mail Received 8 August 2009 revised 6 November 2009 accepted 10 November 2009 doi Antifreeze proteins are structurally diverse polypeptides that have thermal hysteresis activity and have been discovered in many cold-adapted organisms. Of these fungal antifreeze protein has been purified and partially characterized only in a species of psychrophilic basidiomycete Typhula ishikariensis. Here we report a new fungal antifreeze protein from another psychrophile Antarctomyces psychrotrophicus. We examined its biochemical properties and thermal hysteresis activity and compared them with those of the T. ishikariensis antifreeze protein. The antifreeze protein from A. psychrotrophicus was purified and identified as an extracellular protein of approximately 28 kDa which halved in size following digestion with glycosidase. The A. psychrotrophicus antifreeze protein generated bipyramidal ice crystals and exhibited thermal hysteresis activity for example thermal hysteresis C for a mM solution similar to that of fish antifreeze proteins while a unique rugged pattern was

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