title: Identification and characterization of alpha-I-proteinase inhibitor from common carp sarcoplasmic proteins.
abstract: Purification of proteinase inhibitor from common carp (Cyprinus carpio) sarcoplasmic proteins resulted in 2.8% yield with purification fold of 111. Two inhibitors, namely inhibitor I and II, exhibited molecular mass of 47 and 52 kDa, respectively, based on non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both inhibitors I and II were identified to be alpha-1-proteinase inhibitor (α1-PI) based on LC-MS/MS. They were glycoproteins and molecular mass after peptide-N-glycosidase F treatment was 38 and 45 kDa, respectively. The N-glycosylation sites of both inhibitors were determined to be at N214 and N226. The inhibitors specifically inhibited trypsin. The common carp α1-PI showed high thermal stability with denaturation temperatures of 65.43 and 73.31 °C, which were slightly less than those of ovomucoid. High stability toward NaCl was also evident up to 3M. The common carp α1-PI effectively reduced autolytic degradation of bigeye snapper surimi at the concentration as low as 0.025%.
authors: Food Protein Research Unit, School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
authors: Siriphon
authors: S
authors: Siriangkanakun
authors: Food, Nutrition and Health Program, Faculty of Land and Food Systems, The University of British Columbia, 2205 East Mall, Vancouver, British Columbia, Canada.
authors: Eunice C Y
authors: EC
authors: Li-Chan
authors: Food Protein Research Unit, School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand. Electronic address: jirawat@sut.ac.th.
authors: Jirawat
authors: J
authors: Yongsawadigul
mesh_terms: D000818:Animals; D002347:Carps; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008970:Molecular Weight; D012519:Sarcoplasmic Reticulum / Q000737:chemistry*; D014361:Trypsin Inhibitors; D000515:alpha 1-Antitrypsin / Q000032:analysis* / Q000737:chemistry / Q000494:pharmacology
chemical_list: D014361:Trypsin Inhibitors; D000515:alpha 1-Antitrypsin
keywords: Autolytic degradation; Common carp; Glycoprotein; Proteinase inhibitor; Sarcoplasmic proteins