Production and characterization of a cold-active and n-hexane activated lipase from a newly isolated Serratia grimesii RB06-22

UĞUR A., BORAN R.

BIOCATALYSIS AND BIOTRANSFORMATION, cilt.32, sa.4, ss.222-230, 2014 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 4
  • Basım Tarihi: 2014
  • Doi Numarası: 10.3109/10242422.2014.934684
  • Dergi Adı: BIOCATALYSIS AND BIOTRANSFORMATION
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.222-230
  • Anahtar Kelimeler: Serratia grimesii, lipase, n-hexane active, cold active, enzyme characterization, SOLVENT-TOLERANT LIPASE, ORGANIC-SOLVENT, STABLE LIPASE, CHEMICAL-MODIFICATION, ENZYMATIC-HYDROLYSIS, PARTIAL-PURIFICATION, LIPOLYTIC ENZYME, EXPRESSION, MARCESCENS, ALKALINE
  • Gazi Üniversitesi Adresli: Evet

Özet

A lipase-producing bacterium isolated from raw milk was identified as Serratia grimesii based on 16S rRNA sequence analysis. The extracellular lipase was partially purified by ammonium sulfate precipitation and ultrafiltration. Maximal activity was observed at 10 degrees C, the optimum pH was 8.0 and the enzyme was stable at 5-30 degrees C for 1 h. The K-m and V-max values were 1.7 mM and 0.3 mM/min respectively. It was found that the lipase had the highest hydrolytic activity towards sunflower oil and soybean oil. CaCl2 had a stimulatory effect on lipase activity, while EDTA and iodoacetic acid slightly inhibited the lipase activity and the enzyme was strongly inhibited by PMSF. The enzyme was compatible with various non-ionic surfactants as well as sodium cholate and saponin. In addition, the enzyme was relatively stable towards oxidizing agents. This lipase exhibited maximum activity in 35% n-hexane retaining about 2191% activity for 1 h.