The partial purification and properties of pepsin obtained from Turkey proventriculus

Temiz H., Aykut U., Okumus E., Turhan S.

BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, cilt.12, sa.4, ss.450-456, 2007 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 12 Sayı: 4
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1007/bf02931070
  • Dergi Adı: BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.450-456
  • Anahtar Kelimeler: enzyme purification, Turkey proventriculus, pepsin, proteolytic activity, gel filtration, MILK-CLOTTING ENZYME, CYNARA-CARDUNCULUS, CHICKEN PEPSIN, PROTEASES, TEMPERATURE, EXTRACTS, PH
  • Ondokuz Mayıs Üniversitesi Adresli: Evet

Özet

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.