Purification and determination of inhibitory activity of recombinant soyacystatin for surimi application     
Yazarlar (2)
Prof. Dr. Özlem AKPINAR Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Haejung An
University Of Southern California, Amerika Birleşik Devletleri
Makale Türü Özgün Makale
Makale Alt Türü SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale
Dergi Adı Molecular Nutrition and Food Research
Dergi ISSN 1613-4125 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI
Dergi Grubu Q4
Makale Dili İngilizce
Basım Tarihi 03-2005
Cilt No 49
Sayı 3
Sayfalar 247 / 255
DOI Numarası 10.1002/mnfr.200400059
Makale Linki http://doi.wiley.com/10.1002/mnfr.200400059
Özet
A recombinant soyacystatin (r-soyacystatin) was tested for its inhibitory activity against cysteine proteinase of Pacific whiting and its activity was compared to that of egg white cystatin. A recombinant soyacystatin expressed in Escherichia coli was purified to electrophoretic homogeneity using phenylSepharose and DEAE-Sepharose. Native egg white cystatin was purified by using affinity chromatography on CM-papain-Sepharose generated in our lab. Egg white cystatin and soyacystatin were tested for proteinase inhibitory activity against commercial papain and also cathepsin L purified from Pacific whiting muscle. The r-soyacystatin exhibited papain-like protease inhibition activity comparable to that of the egg white cystatin, which could inhibit papain and Pacific whiting cathepsin L. The r-soyacystatin subsequently inhibited the autolytic activity of Pacific whiting surimi. © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Anahtar Kelimeler
Autolytic activity | Egg white cystatin | Pacific whiting | Soyacystatin | Surimi