Partial purification and characterization of almond seed lipase
Küçük Resim Yok
Tarih
2008
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Taylor & Francis Inc
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
A lipase was partially purified from the almond (Amygdalus communis L.) seed by ammonium sulfate fractionation and dialysis. Kinetics of the enzyme activity versus substrate concentration showed typical lipase behavior, with Km and Vmax values of 25mM and 113.63 mu mol min(-1) mg(-1) for tributyrin as substrate. All triglycerides were efficiently hydrolyzed by the enzyme. The partially purified almond seed lipase (ASL) was stable in the pH range of 6-9.5, with an optimum pH of 8.5. The enzyme was stable between 20 and 90 degrees C, beyond which it lost activity progresively, and exhibited an optimum temperature for the hydrolysis of soy bean oil at 65 degrees C. Based on the temperature activity data, the activation energy for the hydrolysis of soy bean oil was calculatedas -5473.6cal/mol. Soy bean oil served as good substrate for the enzyme and hydrolytic activity was enhanced by Ca2+, Fe2+, Mn2+, Co2+, and Ba2+, but strongly inhibited by Mg2+, Cu2+, and Ni2+. The detergents, sodiumdeoxicholate and Triton X-100 strongly stimulated enzyme activity while CTAB, DTAB, and SDS were inhibitors. Triton X-405 had no effect on lipase activity. The partially purified enzyme retained its activity for more than 6 months at -20 degrees C, beyond which it lost activity progressively.
Açıklama
Anahtar Kelimeler
Almond Seed, Characterization, Enzymatic Activity, Lipase, Purification, Stability, Oil, Immobilization, Esterification, Biocatalyst
Kaynak
Preparative Biochemistry & Biotechnology
WoS Q Değeri
Q4
Scopus Q Değeri
Q3
Cilt
38
Sayı
4
