Crab digestive phospholipase: A new invertebrate member

被引:17
作者
Cherif, Slim [1 ]
Ben Bacha, Abir [1 ]
Ben Ali, Yassine [1 ]
Horchani, Habib [1 ]
Rekik, Wiem [1 ]
Gargouri, Youssef [1 ]
机构
[1] ENIS Route Soukra, Lab Biochim & Genie Enzymat Lipases, Sfax 3038, Tunisia
关键词
Crab phospholipase; Hepatopancreas; Purification; Properties; PURIFICATION; DIVERSITY; A(2);
D O I
10.1016/j.biortech.2009.07.031
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
Crab digestive phospholipase (CDPL) was purified from the hepatopancreas of Carcinus mediterraneus crabs. Homogeneous enzyme was obtained after two chromatography steps: anion exchange and size exclusion HPLC column. Homogeneous CDPL has a molecular mass of 14 kDa as determined by SDS/PAGE analysis. Unlike known digestive phospholipases like porcine PLA(2) (PPPL), CDPL displayed its maximal activity at 50 degrees C and not at 37 degrees C. A specific activity of 40 U/mg for the purified CDPL was measured using PC as substrate under optimal conditions (pH 8 and 50 degrees C) in the presence of 8 mM sodium deoxycholate (NaDC) and 10 mM CaCl2. In contrast to PPPL, purified CDPL was completely inactivated at 60 degrees C. The N-terminal sequence was determined by automatic Edman degradation. No similarity between 12 N-terminal amino acid residues of CDPL was found with those of known digestive phospholipases. CDPL appears to be a new member of invertebrate phospholipases, and it is potentially useful for treat phospholipid-rich industrial effluents, or to synthesize useful chemical compounds which can be used in the food industry. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:366 / 371
页数:6
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