Purification and characterization of β-mannanase from Bacillus pumilus (M27) and its applications in some fruit juices

ADIGÜZEL A., NADAROĞLU H., Adiguzel G.

Journal of Food Science and Technology, cilt.52, sa.8, ss.5292-5298, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 52 Sayı: 8
  • Basım Tarihi: 2015
  • Doi Numarası: 10.1007/s13197-014-1609-y
  • Dergi Adı: Journal of Food Science and Technology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.5292-5298
  • Anahtar Kelimeler: Mannanase, Bacillus pumilus (M27), Purification, Characterization, Clarification, LACTIC-ACID BACTERIA, BETA-MANNANASE, ASPERGILLUS-ACULEATUS, RECOMBINANT ENZYME, CULTURE-CONDITIONS, DEGRADING ENZYMES, FERMENTED SAUSAGE, EXPRESSION, GENE, GALACTOSIDASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Thermo alkaline mannanase was purified from the bacteria of Bacillus pumilus (M27) using the techniques of ammonium sulphate precipitation, DEAE-Sephadex ion exchange chromatography and Sephacryl S200 gel filtration chromatography with 111-fold and 36 % yield. It was determined that the enzyme had 2 sub-units including 35 kDa and 55 kDa in gel filtration chromatography and SDS-PAGE electrophoresis systems. The optimum pH and temperature was determined as 8 and 60 A degrees C, respectively. It was also noticed that the enzyme did not lose its activity at a wide interval such as pH 3-11 and at high temperatures such as 90 A degrees C. Additionally, the effects of some metal ions on the mannanase enzyme activity. Moreover, the clarifying efficiency of purified mannanase enzyme with some fruit juices such as orange, apricot, grape and apple was also investigated. Enzymatic treatment was carried out with 1 mL L-1 of purified mannanase for 1 h at 60 A degrees C. It was determined that the highest pure enzyme was efficient upon clarifying the apple juice at 154 % rate.