Purification and characterization of an alkaline pectin lyase produced by a newly isolated Brevibacillus borstelensis (P35) and its applications in fruit juice and oil extraction

Demir N., NADAROĞLU H., Demir Y., Isik C., Taskin E., ADIGÜZEL A., ...Daha Fazla

EUROPEAN FOOD RESEARCH AND TECHNOLOGY, cilt.239, sa.1, ss.127-135, 2014 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 239 Sayı: 1
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1007/s00217-014-2198-8
  • Dergi Adı: EUROPEAN FOOD RESEARCH AND TECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.127-135
  • Anahtar Kelimeler: Pectin lyase, Purification, Brevibacillus borstelensis (P35), Pectin, Juice clarification, Oil extraction, TRANS-ELIMINASE, SOLID-STATE, BACTERIA, STRAIN, MICROORGANISMS, PROTEINS, ENZYMES
  • Atatürk Üniversitesi Adresli: Evet

Özet

An alkaline pectin lyase (PNL) (EC 4.2.2.10) secreted by Brevibacillus borstelensis P35 (GenBank Number: FJ417406) was purified using ammonium sulfate fractionation, anion exchange chromatography on DEAE-cellulose and gel filtration chromatography on Sephadex G-150. The pH and temperature optima of the enzyme were found to be 8.0 and 60 A degrees C. The enzyme does not loose activity up to 60 A degrees C if exposed for 1 h. The values of K (m) and V (max) of the enzyme were 0.625 mg/mL and 126.32 s(-1), respectively. The molecular weight was found to be 36 +/- A 01 kDa. The presence of 10 mM concentration of Ca2+, Cu2+, Mn2+, Mg2+, Zn2+, Hg2+, Fe2+ and EDTA, l-cystein, ascorbic acid significantly enhanced the PNL of the purified enzyme. In the course of the laboratory trials, it was demonstrated that PNL from B. borstelensis (P35) could be successfully applied to the production and clarification of fruit juice and oil extraction.