Production and characterization of a cold-active and n-hexane activated lipase from a newly isolated Serratia grimesii RB06-22
Yükleniyor...
Dosyalar
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Taylor & Francis
Erişim Hakkı
info:eu-repo/semantics/embargoedAccess
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.
Açıklama
Anahtar Kelimeler
Serratia Grimesii, Lipase, N-hexane Active, Cold Active, Enzyme Characterization
Kaynak
Biocatalysis and Biotransformation
WoS Q Değeri
N/A
Scopus Q Değeri
Q2
Cilt
32
Sayı
4
