Thermodynamic activation and structural analysis of trypsin I from Monterey sardine (Sardinops sagax caerulea)

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• 作者：Aldo A. Arvizu-Flores^a ; Idania E. Quintero-Reyes^a ; Martha Felix-Lopez^b ; Maria A. Islas-Osuna^b ; ¹ ; Gloria Yepiz-Plascencia^b ; Ramó ; n Pacheco-Aguilar^b ; Arti Navare^c ; Facundo M. Ferná ; ndez^c ; Enrique F. Velazquez-Contreras^a ; Rogerio R. Sotelo-Mundo^b ; ^rrs@ciad.mx ; Francisco J. Castillo-Yañ ; ez^a ; ^{jcastillo@guayacan.uson.mx}
• 关键词：Trypsin ; Cold-adapted ; Monterey sardine ; Thermodynamic activation parameters ; Sardinops sagax caerulea ; Molecular modelling ; cDNA
• 刊名：Food Chemistry
• 出版年：2012
• 期刊代码：48_03088146
• 类别：abs
• 出版时间：1 August, 2012
• 卷：133
• 期：3
• 页码：898-904
• 文件大小：1101 K

摘要

In this work, we report the molecular characterisation of trypsin I (Try I) from Monterey sardine (Sardinops sagax caerulea). Aspects such as thermodynamic activation parameters, molecular model and cDNA-deduced amino acid sequence allow a more in depth understanding of its activity at low temperatures. The analysis of the thermodynamic activation parameters suggests that this molecule is a cold-adapted protease. From the molecular cloning, we deduced the amino acid sequence and predicted a theoretical structural model of sardine Try I with a classical trypsin fold. Cold-adaptation of this enzyme probably comes from amino acid replacement of key residues to improve flexibility at low temperature, thus increasing k_cat. The cold-adaptation of sardine Try I opens a wide range of biotechnological applications for this protease and also it is interesting from the structure function relationship point of view of serine protease proteins.