The partial purification and properties of pepsin obtained from Turkey proventriculus |
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Authors: | Hasan Temiz Umut Aykut Emin Okumus Sadettin Turhan |
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Institution: | 1.Department of Food Engineering, Engineering Faculty,Ondokuz Mayis University,Samsun,Turkey;2.Department of Chemical Engineering, Engineering Faculty,Ondokuz Mayis University,Samsun,Turkey |
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Abstract: | 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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