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(A) Chromatography of RP-HPLC using a C18 column and (B) SDS-PAGE profile (15%) of purified Cc-PLA 2 -II. Lane 1: molecular mass markers, lanes 2 and 3: purified Cc-PLA 2 -II, land 4: Wa-PLA 2 -II. Blue line indicates linear acetonitrile gradient. (C) MALDI-TOF spectrum of Cc-PLA 2 -II.
Source publication
Secreted phospholipases A2 are snake-venom proteins with many biological activities, notably anti-tumor activity. Phospholipases from the same snake type but different geographical locations have shown similar biochemical and biological activities with minor differences in protein sequences. Thus, the discovery of a new phospholipase A2 with unique...
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Snake venom is an ecologically-relevant functional trait directly linked with a snake’s fitness and survival, facilitating predation and defense. Snake venom variation occurs at all taxonomic levels, but the study of variation at intraspecific level is still in its early stages. The common adder ( Vipera berus ) exhibits considerable variation in c...
Citations
... 2 PLA 2 enzymes are abundant in several biological tissues and liquids; among them is the viperidea venom. 3 According to their molecular weight, primary sequences, number and position of disulfide bonds, and their requirement of calcium for catalytic activity, five PLA 2 classes are defined: cytosolic calciumdependent (cPLA 2 ), calcium-independent (iPLA 2 ), plateletactivating factor (PAF) acetylhydrolase, lysosomal PLA 2 , and secreted PLA 2 (sPLA 2 ). 2 The sPLA 2 of snake venom is characterized by a molecular weight ranging from 14 to 18 kDa and high content on disulfide (S−S) bonds (5−8). 2 Their homology in the primary sequences and disulfide bonding pattern allow to class them onto two groups I and II. sPLA 2 group I is found in viperidea venom or Elapidae, and Hydrophidae snake venoms are rich with sPLA 2 group II. 3 A broad range of biological processes involving snake venom sPLA 2 such as anticoagulant, antibacterial, antitumoral, and antiangiogenic activities makes these enzymes a potential pharmacological target. ...
... sPLA 2 group I is found in viperidea venom or Elapidae, and Hydrophidae snake venoms are rich with sPLA 2 group II. 3 A broad range of biological processes involving snake venom sPLA 2 such as anticoagulant, antibacterial, antitumoral, and antiangiogenic activities makes these enzymes a potential pharmacological target. Moreover, snake venom sPLA 2 have been used in several industrial applications as biocatalysts especially biodiesel production, organic synthesis, and processing of vegetable oils. ...
... Enzymatic degumming, which is commonly conducted with phospholipases, exhibited numerous advantages, for instance, ameliorating the process yield, decreasing the level of wastewater, alkali, and acid, and reducing the industrial operating costs, and negative impacts on the environment. 3,5,7 Among phospholipases, sPLA 2 are among the most effective degumming candidates as they convert nonhydratable PLs into their hydratable forms (lysoPLs). 1, 8,9 Soybean oil, the most widely consumed vegetable oil, was used in this study to assess the performance of free and immobilized WaPLA 2 -I and WaPLA 2 -II in the degumming process by measuring the phosphorus content. ...
Enzymatic degumming utilizing phospholipase enzymes could be used in ecologically friendly procedures with enhanced oil recovery yields. In this study, two phospholipases A2 of group I and II, WaPLA2-I and WaPLA2-II, from the snake venom of Saudi Walterinnesia aegyptia were evaluated for soybean oil degumming after being immobilized on three different support materials (calcium alginate (CA), CA-gelatin (CAG), and CA-chitosan (CAC), and cross-linked with glutaraldehyde). Higher yields of CAC-immobilized PLA2-I (85 ± 3%) and PLA2-II (87 ± 3.6%) compared to CAG (77.3 ± 2.1 and 79 ± 2.6%, respectively) and CA beads (55.7 ± 2.5% and 57.3 ± 3.1%, respectively) were observed. In addition, the optimal temperature of immobilized WaPLA2-I and WaPLA2-II increased from 45 to 55 °C and from 55 to 65 °C, respectively. Their stability at high temperatures was also significantly enhanced covering a larger range (70–80 °C). Likewise, the pH/activity profile of WaPLA2 was greatly expanded upon immobilization with the pH-optima being shifted by 0.5 to 1 pH unit to the basic side. Similarly, the stability of WaPLA2s in the presence of organic solvents was also significantly improved, while the affinity for calcium and bile salt was the same for both free and immobilized enzymes. Interestingly, the remaining activity of immobilized WaPLA2 onto different supports was more than 50 or 60% after eight recycles or 120 days of storage at 4 °C, respectively. CAC–WaPLA2-II was the best immobilized enzyme complex for the oil degumming process by reducing its final residual phosphorus content from 168 mg/kg to less than 10 mg/kg in only 4 h. Overall, CAC–WaPLA2-II showed the most attractive profiles of temperature, pH, and reaction duration as well as significant storage stability and reusability.
