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KMID : 1094720070120040450
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Biotechnology and Bioprocess Engineering
2007 Volume.12 No. 4 p.450 ~ p.456
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The partial purification and properties of pepsin obtained from Turkey proventriculus
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Temiz Hasan
Aykut Umut
Okumus Emin
Turhan Sadettin
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Abstract
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In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1?2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SDS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results.
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KEYWORD
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enzyme purification, turkey proventriculus, pepsin, proteolytic activity, gel filtration
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