TY  - JOUR
T1  - Purification and Characterization of Lipase from the Liver of Carp, Cyprinus carpio L. (1758), Living in Lake Tödürge (Sivas, TÜRKİYE)
TT  - Purification and Characterization of Lipase from the Liver of Carp, Cyprinus carpio L. (1758), Living in Lake Tödürge (Sivas, TÜRKİYE)
AU  - Görgün, Salih
AU  - Akpınar, Mehmet Ali
PY  - 2012
DA  - April
JF  - Turkish Journal of Fisheries and Aquatic Sciences
PB  - Trabzon Su Ürünleri Merkez Araştırma Enstitüsü
WT  - DergiPark
SN  - 1303-2712
VL  - 12
IS  - 2
LA  - tr
AB  - In this study, a lipase from the liver of Cyprinus carpio Linnaeus (1758) living in Tödürge Lake (Sivas) was purified with purification parameters of 90.38 μmol/dk.mg protein specific activity and 75.50 fold purity. The purification procedure  consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively. The purified lipase showed a single band with approximately a molecular weight of 74 kDa by sodium dodecyl sulfate-polyacrylamide gel  electrophoresis (SDS-PAGE). pH and temperature optimums for the purified enzyme were determined as 8.0 and 37 °C using  p-nitrophenyl butirate (p-NPB) as substrate. Km and Vmax values were found as 0.17 mM p-NPB and 2.6 μmol/mL.dk, respectively. It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.
KW  - Cyprinus carpio
KW  - lipase activity
KW  - Q sepharose
KW  - sephacryl S 200 HR
KW  - phenyl sepharose CL-4B
KW  - Tödürge Lake
N2  - In this study, a lipase from the liver of Cyprinus carpio Linnaeus (1758) living in Tödürge Lake (Sivas) was purified with purification parameters of 90.38 μmol/dk.mg protein specific activity and 75.50 fold purity. The purification procedure  consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively. The purified lipase showed a single band with approximately a molecular weight of 74 kDa by sodium dodecyl sulfate-polyacrylamide gel  electrophoresis (SDS-PAGE). pH and temperature optimums for the purified enzyme were determined as 8.0 and 37 °C using  p-nitrophenyl butirate (p-NPB) as substrate. Km and Vmax values were found as 0.17 mM p-NPB and 2.6 μmol/mL.dk, respectively. It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.
UR  - https://dergipark.org.tr/en/pub/trjfas-ayrildi/issue//160250
L1  - https://dergipark.org.tr/en/download/article-file/141620
ER  -