Some biochemical properties of lipase from bay laurel (Laurus nobilis L.) seeds
Küçük Resim Yok
Tarih
2008
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Wiley
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Lipase was isolated from bay laurel (Laurus nobilis L.) seeds, some biochemical properties were determined. The bay laurel oil was used as the substrate in all experiments. The pH optimum was found to be 8.0 in the presence of this substrate. The temperature optimum was 50 degrees C. The specific activity of the lipase was found to be 296 U mg protein(-1) in optimal conditions. The enzyme activity is quite stable in the range of pH 7.0-10. The enzyme was stable for 1 h at its optimum temperature, and retained about 68% of activity at 60 degrees C during this time. K-m and V-max values were determined as 0.975 g and 1.298 U mg protein(-1), respectively. Also, storage stability and metal effect on lipolytic activity were investigated. Enzyme activity was maintained for 9, 12, and 42 days at room temperature, 4 and -20 degrees C, respectively. Ca2+, Co2+, Cu2+, Fe2+, and Mg2+ lightly enhanced bay laurel lipase activity.
Açıklama
Anahtar Kelimeler
Bay Laurel (Laurus Nobilis L.), Lipase, Defatting, Thermal Stability, Metal Ions, Extracts, Latex, Interesterification, Purification
Kaynak
Journal Of The American Oil Chemists Society
WoS Q Değeri
Q2
Scopus Q Değeri
Q2
Cilt
85
Sayı
3
