Purification and biochemical properties of Hexaplex trunculus digestive lipase

Zarai, Zied; Ali, Madiha Bou; Fendri, Ahmed; Louati, Hanen; Mejdoub, Hafedh; Gargouri, Youssef

doi:10.1016/j.procbio.2012.10.004

Cited by 16 publications

(14 citation statements)

References 28 publications

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“…), green marine snail (Zarai et al . ) and pancreatic (Verger ) lipases for which the presence of the substrate increases the thermostability of the lipolytic enzymes.…”

Section: Resultsmentioning

confidence: 99%

“…Like GmDL (Smichi et al 2013), 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 2007;Zarai et al 2012).…”

Section: Effect Of Ph and Temperature On Gmde Activity And Stabilitymentioning

confidence: 94%

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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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“…), green marine snail (Zarai et al . ) and pancreatic (Verger ) lipases for which the presence of the substrate increases the thermostability of the lipolytic enzymes.…”

Section: Resultsmentioning

confidence: 99%

Section: Effect Of Ph and Temperature On Gmde Activity And Stabilitymentioning

confidence: 94%

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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“…Aryee et al [6] reported that lipase form grey mullet viscera was active within the temperature range of 20-60°C. Zarai et al [25] found that thermal stability of the marine snail digestive lipase retained about 85% of its maximum activity after incubation for 30 min at 50°C and when the enzyme was incubated at 65°C, it was completely inactive.…”

Section: Ph and Temperature Profilesmentioning

confidence: 99%

Laundry detergent-stable lipase from Pacific white shrimp (Litopenaeus vannamei) hepatopancreas: Effect of extraction media and biochemical characterization

Kuepethkaew

Sangkharak

Benjakul

et al. 2016

International Journal of Food Properties

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Extraction and biochemical properties of a new lipase from the hepatopancreas of Pacific white shrimp were studied. Recovery of the hepatopancreas powder with 50 mM Tris-HCl, pH 7.0 containing 0.2% (v/v) Brij35 gave a higher recovery of lipase activity than other extractants tested (p < 0.05). The optimal pH and temperature for lipase activity were 8.5 and 60°C, respectively, when p-nitrophenyl palmitate was used as a substrate. The enzyme was stable to heat treatment up to 40°C and over a pH range of 7.0-10.0 for 30-120 min. Lipase activities continuously decreased as the sodium deoxycholate (NaDC) concentration increased, but activities increased as NaCl concentration increased up to 3.0 M. Hydrolytic activity was enhanced by NaN 3 , but strongly inhibited by Hg 2+ , Cu 2+ , Al 3+ , and phenylmethanesulfonyl fluoride. The lipase was evaluated as highly stable against surfactants (Tween 20, Tween 80, Triton X-100, and gum arabic). However, the enzyme was unstable against sodium dodecyl sulphate. Stability of the lipase with commercial liquid and solid detergents (Attack ® , Bres ® , Omo ® , and Pao ®) was also investigated. The lipase exhibited substantial stability and compatibility with tested commercial liquid and solid laundry detergents for 30-60 min. The overall properties of the lipase from Pacific white shrimp hepatopancreas, thus leading us to propose that it is an excellent candidate for use as biocatalysts for better detergent formulation.

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“…The turkey pancreatic lipase (TPL) shows the same features of HPL, and its three-dimensional structure consists of two domains stabilized by six disulphide bridges [8]. Moreover, other studies have reported new enzymes isolated from aquatic species with interesting potential in food processing [3,[19][20][21]. To provide an overview on pancreatic lipases, we have tried to extend our research on the fish lipolytic system in order to understand the evolutionary aspects of fish lipases as compared to those of mammals.…”

Section: Introductionmentioning

confidence: 99%

“…The Sparidae family has been considered with regard to lipolytic enzymes involved in lipid digestion; Smichi et al [24] have purified a lipase from the annular seabream (AsDL). The characterized enzyme shows distinct properties to TPL [8] and lipases from other marine species [19,21]. From the same family, a lipase from the red seabream has been isolated and purified and its functional properties have been performed to explain the differences with pancreatic lipases [25].…”

Section: Introductionmentioning

confidence: 99%

Dissecting the Interaction Deficiency of a Cartilaginous Fish Digestive Lipase with Pancreatic Colipase: Biochemical and Structural Insights

Achouri

Tomàs-Gamisans

Triki-Fendri

et al. 2020

BioMed Research International

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A full-length cDNA encoding digestive lipase (SmDL) was cloned from the pancreas of the smooth-hound (Mustelus mustelus). The obtained cDNA was 1350 bp long encoding 451 amino acids. The deduced amino acid sequence has high similarity with known pancreatic lipases. Catalytic triad and disulphide bond positions are also conserved. According to the established phylogeny, the SmDL was grouped with those of tuna and Sparidae lipases into one fish digestive lipase cluster. The recently purified enzyme shows no dependence for bile salts and colipase. For this, the residue-level interactions between lipase-colipase are yet to be clearly understood. The structural model of the SmDL was built, and several dissimilarities were noticed when analyzing the SmDL amino acids corresponding to those involved in HPL binding to colipase. Interestingly, the C-terminal domain of SmDL which holds the colipase shows a significant role for colipase interaction. This is apt to prevent the interaction between fish lipase and the pancreatic colipase which and can provide more explanation on the fact that the classical colipase is unable to activate the SmDL.

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Purification and biochemical properties of Hexaplex trunculus digestive lipase

Cited by 16 publications

References 28 publications

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

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

Laundry detergent-stable lipase from Pacific white shrimp (Litopenaeus vannamei) hepatopancreas: Effect of extraction media and biochemical characterization

Dissecting the Interaction Deficiency of a Cartilaginous Fish Digestive Lipase with Pancreatic Colipase: Biochemical and Structural Insights

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