A grey mullet enzyme displaying both lipase and phospholipase activities: Purification and characterization

Smichi, Nabil; Gargouri, Youssef; Miled, Nabil; Fendri, Ahmed

doi:10.1016/j.ijbiomac.2013.03.056

Cited by 28 publications

(45 citation statements)

References 45 publications

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“…The purification flow sheet is given in Table 2. The specific activity of pure SPL reached a maximum of 5300 U/mg when tributyrin was used as substrate at pH 8.5 and 40°C in the Golden grey mullet (Mugil auratus) 100 - [31] Porcine 13,000 10,400 [32,33] One lipase unit corresponds to 1 μmol of fatty acid liberated per minute. One colipase unit corresponds to the amount of the cofactor that increases bile salts inhibited pancreatic lipase activity by one enzyme unit.…”

Section: Purification and Characterization Of Splmentioning

confidence: 99%

Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca)

Bouchaala¹,

Ali²,

Miled³

et al. 2015

Appl Biochem Biotechnol

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In order to identify fish enzymes displaying novel biochemical properties, we have chosen the common stingray (Dasyatis pastinaca), one of the most primitive living jawed aquatic vertebrates as a starting biological material to purify a lipase. A stingray pancreatic lipase (SPL) was purified from delipidated pancreatic powder. The SPL molecular weight was around 55 kDa which is slightly higher than that of known classical pancreatic lipases (50 kDa). This increase in the molecular weight was due to glycosylation. Like classic pancreatic lipases, SPL was found to be much more active on short-chain triacylglycerols than on long-chain ones. Natural detergents act as inhibitors of the SPL activity. This inhibition can be reversed by the addition of stingray colipase. Starting from total pancreatic messenger RNAs (mRNAs), partial stingray pancreatic lipase complementary DNA (cDNA) was synthesized by reverse transcriptase-polymerase chain reaction (RT-PCR) and cloned into the PGEM-T vector. Partial amino acid sequence of the SPL was homologous to that of Japanese eel, porcine, and human pancreatic lipases. A 3D structure model of the sequenced part of SPL was built using the 3D structure of porcine pancreatic lipase as template, since both lipases shared an amino acid sequence identity of 60%.

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Section: Purification and Characterization Of Splmentioning

confidence: 99%

Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca)

Bouchaala¹,

Ali²,

Miled³

et al. 2015

Appl Biochem Biotechnol

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“…As in the case with grey mullet lipase (Smichi et al . ), the purified esterase was mostly active between pH 7 and 9 with an optimum at pH 8 (Fig. A).…”

Section: Resultsmentioning

confidence: 86%

“…This value is higher than that of the lipase previously purified from the viscera of the same species ( M. auratus ) (35 kDa) (Smichi et al . ). The molecular mass value was in line with the one determined by gel filtration analysis.…”

Section: Resultsmentioning

confidence: 97%

“…Like GmDL (Smichi et al . ), the activity of GmDE increased with temperature and reached its maximum value at 50C. Most digestive lipases from marine sources, described so far, are not thermoactive except for few enzymes, such as crab digestive and marine green snail lipases (Cherif et al .…”

Section: Resultsmentioning

confidence: 97%

“…This lipase has a wide spectrum of substrate specificity as it hydrolyzes short‐chain and long‐chain triacylglycerols as well as phospholipids at comparable rates (Smichi et al . ).…”

Section: Introductionmentioning

confidence: 97%

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A High Salt-Tolerant Thermoactive Esterase from Golden Grey Mullet: Purification, Characterization and Kinetic Properties

Smichi¹,

Fendri²,

Gargouri³

et al. 2015

Journal of Food Biochemistry

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An esterase was purified from the golden grey mullet viscera using successively a Sephacryl S-100 gel filtration, an anion-exchange chromatography and a highperformance liquid chromatography filtration column. The pure esterase (GmDE) is a monomer that has a molecular mass of about 55 kDa, as determined by SDS-PAGE analysis. The purified enzyme displayed a specific activity of 100 U/mg on short-chain triacylglycerols at a temperature of 50C. GmDE is therefore a thermoactive enzyme as compared to other fish lipolytic enzymes that have been studied so far. No significant lipolytic activity was noticed when long-chain triacylglycerol (olive oil) was used as a substrate. It is worth noting that the pure esterase was active in the presence of salt concentrations as high as 0.8 M. The GmDE N-terminal amino acid sequence showed no similarities with that of other known fish esterases. Altogether, these results suggest that the GmDE is a member of a new group of digestive esterases belonging to vertebrates. PRACTICAL APPLICATIONSCharacterization of an esterase from low-value fish viscera and the use of digestive enzyme may add value to this discarded species. Furthermore, the activity and stability at alkaline pH may also find use in laundry detergents. The thermoactivity of the purified esterase makes it a good candidate for potential application in food processing operations. Finally, the stability of the enzyme in high salt concentrations suggests that it can be used as an additive in different processes (food, cosmetic and pharmaceutical operations).

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Byproducts from Fish Harvesting and Processing

Benjakul¹,

Sae‐leaw²,

Simpson³

2019

Byproducts From Agriculture and Fisheries

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A grey mullet enzyme displaying both lipase and phospholipase activities: Purification and characterization

Cited by 28 publications

References 45 publications

Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca)

Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca)

A High Salt-Tolerant Thermoactive Esterase from Golden Grey Mullet: Purification, Characterization and Kinetic Properties

Byproducts from Fish Harvesting and Processing

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