The partial purification and properties of pepsin obtained from Turkey proventriculus

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 SIDS-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. (c) KSBB.