FRACTIONATION AND CHARACTERIZATION OF CYSTEINE PROTEINASE INHIBITOR FROM CHICKEN PLASMA |
| |
| Authors: | SAROAT RAWDKUEN SOOTTAWAT BENJAKUL WONNOP VISESSANGUAN TYRE C LANIER |
| |
| Affiliation: | Department of Food Technology Faculty of Agro-Industry Prince of Songkla University Hat Yai, 90112, Thailand; National Center for Genetic Engineering and Biotechnology National Science and Technology Development Agency 113 Phaholyothin Road, Klong1, Klong Luang Pathumthani, 12120, Thailand; Department of Food Science North Carolina State University Raleigh, NC 27695-7624 |
| |
| Abstract: | The fractionation of cysteine proteinase inhibitor (CPI) from chicken blood plasma was carried out using polyethylene glycol‐4000 or ammonium sulfate (AS) precipitation. The addition of PEG at the level of 400 g/L, on the basis of the original volume of plasma protein, was more effective to fractionate CPI than using AS. CPI in the PEG fraction had a molecular weight of about 46 kDa with intramolecular disulfide bond. CPI containing fraction was colorless and had no absorbance in the range of 700–360 nm. The fraction was stable in the temperature range of 40–90C for 10 min and still retained high inhibitory activity toward papain after incubation at 90C for 60 min. NaCl, at 0–3.0% concentration, did not affect the inhibitory activity of the CPI containing fraction. The fraction was stable at pH 8.0, and the minimal inhibitory activity against papain was found at pH 5–6. Therefore, PEG fractionation effectively isolated the CPI from chicken plasma. |
| |
| Keywords: | |
|
|
