Background: Middle East respiratory syndrome coronavirus (MERS-CoV) causes viral pneumonia diseas... more Background: Middle East respiratory syndrome coronavirus (MERS-CoV) causes viral pneumonia disease in humans. The close contact with camels and drinking milk may cause Middle East respiratory syndrome coronavirus transfer to humans. Methods: This study was designed to detect the existence of Middle East respiratory syndrome coronavirus in camel milk samples collected from healthy animals according to local customs from 83 barns located around Saudi Arabia. Camel milk samples were examined for viral RNA by RT-qPCR, also ELISA assay was performed to detect IgG antibodies directed against MERS Receptor-Binding Protein (RBD).Results: Among 83 camel milk samples tested,the result showed that seven samples (8.4%) were positive for MERS-CoV RNA, while 40.9% of camel milk samples had antibodies directed against this virus.Conclusions: The findings indicate that some regions (East and South part) are characterized by a high incidence of viral antibodies. The South western region displayed th...
Journal of microbiology, biotechnology and food sciences, 2016
The present work aimed to optimize a molasses and tuna-processing by-products based new economic ... more The present work aimed to optimize a molasses and tuna-processing by-products based new economic medium for biosurfactant (BS) production by a promising strain of Aneurinibacillus migulanus. A culture medium based on a mixture of molasses and supernatants generated from tuna by-products supplemented with oligoelements solution was optimized using the mixture design methodology. Biosurfactant (BS) production and emulsification index (E24) were evaluated. Maximal BS of 2.95 g/l was obtained with a 95:5 (v:v) mixture of molasses and tuna by-product supernatant. However, higher level of E24 (62%) was recorded with medium containing the proportion 5:95 (v:v) of molasses and tuna by-product supernatant. The predicted responses from these mixture proportions were also validated experimentally. Interestingly, oligoelements supplements were not needed to prepare the culture medium. Molasses and tuna-by-product, non-conventional substrates, can be used efficiently for BS production by A. migu...
The condensation of several primary amines and diamines with various N-ethoxycarbonyles N-tosylhy... more The condensation of several primary amines and diamines with various N-ethoxycarbonyles N-tosylhydrazonates (1a-b), triazolones (2) and bis-triazolone (3) resulted in ethanol under ultrasound irradiation. Compared with the conventional methods, the main advantages of the present procedure are milder conditions, shorter reaction time and higher yields. The newly synthesized compounds were evaluated for angiotensin I-converting enzyme (ACE) inhibition. The results were compared to Captopril as a reference drug. Compounds 3b, 2h, 3a, 2d, and 2f showed not only inhibition activity with IC values of 0.162, 0.253, 0.253, 0.281 and 0.382 µM, respectively, but also minimal toxicity. The docking of chemical compounds in the ACE active site showed possible inhibitory effect of all compounds on the catalytic activity of the enzyme, which would satisfactorily explain the anti-hypertensive effect of these compounds.
Here we report the cDNA cloning of a phospholipase A (PLA) from five Sparidae species. The deduce... more Here we report the cDNA cloning of a phospholipase A (PLA) from five Sparidae species. The deduced amino acid sequences show high similarity with pancreatic PLA. In addition, a phylogenetic tree derived from alignment of various available sequences revealed that Sparidae PLA are closer to avian PLA group IB than to mammals' ones. In order to understand the structure-function relationships of these enzymes, we report here the recombinant expression in E.coli, the refolding and characterization of His-tagged annular seabream PLA (AsPLA). A single Ni-affinity chromatography step was used to obtain a highly purified recombinant AsPLA with a molecular mass of 15kDa as attested by gel electrophoresis and MALDI-TOF mass spectrometry data. The enzyme has a specific activity of 400U.mg measured on phosphatidylcholine at pH 8.5 and 50°C. The enzyme high thermo-activity and thermo-stability make it a potential candidate in various biological applications. The 3D structure models of these enzymes were compared with structures of phylogenetically related pancreatic PLA. By following these models and utilizing molecular dynamics simulations, the resistance of the AsPLA at high temperatures was explained. Using the monomolecular film technique, AsPLA was found to be active on various phospholipids spread at the air/water interface at a surface pressure between 12 and 25dyncm. Interestingly, this enzyme was shown to be mostly active on dilauroyl-phosphatidylglycerol monolayers and this behavior was confirmed by molecular docking and dynamics simulations analysis. The discovery of a thermo-active new member of Sparidae PLA, provides new insights on structure-activity relationships of fish PLA.
International Journal of Biological Macromolecules, 2017
In order to identify fish enzymes displaying novel biochemical properties, we choose the common s... more In order to identify fish enzymes displaying novel biochemical properties, we choose the common smooth-hound (Mustelus mustelus) as a starting biological material to characterize the digestive lipid hydrolyzing enzyme. A smooth-hound digestive lipase (SmDL) was purified from a delipidated pancreatic powder. The SmDL molecular weight was around 50kDa. Specific activities of 2200 and 500U/mg were measured at pH 9 and 40°C using tributyrin and olive oil emulsion as substrates, respectively. Unlike known mammal pancreatic lipases, the SmDL was stable at 50°C and it retained 90% of its initial activity after 15min of incubation at 60°C. Interestingly, bile salts act as an activator of the SmDL. It's worth to notice that the SmDL was also salt-tolerant since it was active in the presence of high salt concentrations reaching 0.8M. Fatty acid (FA) analysis of oil from the smooth-hound viscera showed a dominance of unsaturated ones (UFAs). Interestingly, the major n-3 fatty acids were DHA and EPA with contents of 18.07% and 6.14%, respectively. In vitro digestibility model showed that the smooth hound oil was efficiently hydrolyzed by pancreatic lipases, which suggests the higher assimilation of fish oils by consumers.
Journal of agricultural and food chemistry, Jan 22, 2017
Novel phospholipase (PLA2) genes from the Sparidae family were cloned. The sequenced PLA2 reveale... more Novel phospholipase (PLA2) genes from the Sparidae family were cloned. The sequenced PLA2 revealed an identity with pancreatic PLA2 group IB. To better understand the structure/function relationships of these enzymes and their evolution, the Diplodus annularis PLA2 (DaPLA2) was overexpressed in E. coli. The refolded enzyme was purified by Ni-affinity chromatography and has a molecular mass of 15 kDa as determined by MALDI-TOF spectrometry. Interestingly, unlike the pancreatic type, the DaPLA2 was active and stable at higher temperatures, which suggests its great potential in biotechnological applications. The 3D structure of DaPLA2 was constructed to gain insights into the functional properties of sparidae PLA2. Molecular docking and dynamic simulations were performed to explain the higher thermal stability and the substrate specificity of DaPLA2. Using the monolayer technique, the purified DaPLA2 was found to be active on various phospholipids ranging from 10 to 20 mN·m(-1), which ...
ABSTRACT An esterase was purified from the golden grey mullet viscera using successively a Sephac... more ABSTRACT An esterase was purified from the golden grey mullet viscera using successively a Sephacryl S-100 gel filtration, an anion-exchange chromatography and a high-performance 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).
ABSTRACT A highly thermostable and alkaline lichenase was isolated from the newly isolated strain... more ABSTRACT A highly thermostable and alkaline lichenase was isolated from the newly isolated strain Bacillus UEB-S. A single step purification was achieved by heating the enzyme extract for 30 min at 90 °C. The enzyme was a monomeric protein with a molecular weight of 28 kDa. The optimal temperature and pH for UEB-S lichenases activity were 60 °C and 6.0, respectively. More remarkably, the purified lichenase was stable over a broad range of temperature and pH. It retained more than 60% of its activity after incubation at 90 °C for 30 min. Substrate specificity studies revealed that the enzyme is a true lichenase. A genomic library was screened. It allows the identification of a gene that encodes a putative lichenase showing 98% identity with the lichenase from Bacillus subtilis 168. Sequence comparison revealed that the two enzymes differed by two mutations at positions 69 and 83, where Val 69 and Ser 83are replaced by Met and Ala amino acids, respectively. Therefore, a theoretical structural model was built using the lichenase from Bacillus subtilis 168 Pdb code (3o5sA) structure as template. Comparison of the two 3D structures suggested that Val 69 stabilizes a calcium binding site and could be involved in the higher stability of the enzyme.
In order to identify fish enzymes displaying novel biochemical properties, we have chosen the com... more 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 %.
... In vitro, the max-155 9 Digestive Lipases Inhibition: an In vitro Study Ali Tiss, Nabil Miled... more ... In vitro, the max-155 9 Digestive Lipases Inhibition: an In vitro Study Ali Tiss, Nabil Miled, Robert Verger, Youssef Gargouri, and Abdelkarim Abousalham Lipases and Phospholipases in Drug Development: From Biochemistry to Molecular Pharmacology. ...
European Journal of Lipid Science and Technology, 2015
ABSTRACT Using lipid emulsions as well as the monomolecular film technique, we studied some kinet... more ABSTRACT Using lipid emulsions as well as the monomolecular film technique, we studied some kinetic properties of sardine digestive lipase (SaDL). The pure lipase was able to hydrolyse a triolein emulsion in the absence of any additives and seems therefore to tolerate the accumulation of long free fatty acids at the interface. The kinetic behaviour of SaDL can be explained by the high penetration capacity of this enzyme into a lipidic interface. SaDL hydrolyzes efficiently pure tributyrin, in the absence of additives. Subsequently, the sardine lipase is not denaturated at high interfacial energy. A kinetic study of the surface pressure dependency of the regioselectivity of SaDL was performed using an optically pure stereoisomer of diglyceride (1,2-sn dicaprin) and a prochiral isomer (1,3-sn-dicaprin) that were spread as monomolecular films at the air-water interface. At low surface pressure, SaDL acts preferentially on distal carboxylic ester groups of the diglyceride isomer (1,3-sn-dicaprin) but at high surface pressure, this enzyme prefers adjacent ester groups of the (1,2-sn-dicaprin) isomer. Interestingly, the sardine digestive lipase was found to hydrolyse efficiently the secondary ester group of a triglyceride analog. This is in line with the fact that SaDL hydrolysed triolein at the sn-2 position, as shown using the thin-layer chromatography technique. This property is sought for the synthesis of specific triacylglycerol-based compounds, such as structured lipids.
Abstract: Turkey pancreatic lipase immobilized on celite was used to produce fatty acids, diacylg... more Abstract: Turkey pancreatic lipase immobilized on celite was used to produce fatty acids, diacylglycerols and monoacylglycerols by hydrolysis of palm olein in a solvent free system. Turkey lipase preparation was obtained out of a delipidated pancreatic for a biotechnological application. The effect of process variables on enzymatic hydrolysis was investigated, and the maximization of hydrolysis rate was carried out using an experimental design technique. A high degree of hydrolysis (71.85±1.618%) was reached under ...
Background: Middle East respiratory syndrome coronavirus (MERS-CoV) causes viral pneumonia diseas... more Background: Middle East respiratory syndrome coronavirus (MERS-CoV) causes viral pneumonia disease in humans. The close contact with camels and drinking milk may cause Middle East respiratory syndrome coronavirus transfer to humans. Methods: This study was designed to detect the existence of Middle East respiratory syndrome coronavirus in camel milk samples collected from healthy animals according to local customs from 83 barns located around Saudi Arabia. Camel milk samples were examined for viral RNA by RT-qPCR, also ELISA assay was performed to detect IgG antibodies directed against MERS Receptor-Binding Protein (RBD).Results: Among 83 camel milk samples tested,the result showed that seven samples (8.4%) were positive for MERS-CoV RNA, while 40.9% of camel milk samples had antibodies directed against this virus.Conclusions: The findings indicate that some regions (East and South part) are characterized by a high incidence of viral antibodies. The South western region displayed th...
Journal of microbiology, biotechnology and food sciences, 2016
The present work aimed to optimize a molasses and tuna-processing by-products based new economic ... more The present work aimed to optimize a molasses and tuna-processing by-products based new economic medium for biosurfactant (BS) production by a promising strain of Aneurinibacillus migulanus. A culture medium based on a mixture of molasses and supernatants generated from tuna by-products supplemented with oligoelements solution was optimized using the mixture design methodology. Biosurfactant (BS) production and emulsification index (E24) were evaluated. Maximal BS of 2.95 g/l was obtained with a 95:5 (v:v) mixture of molasses and tuna by-product supernatant. However, higher level of E24 (62%) was recorded with medium containing the proportion 5:95 (v:v) of molasses and tuna by-product supernatant. The predicted responses from these mixture proportions were also validated experimentally. Interestingly, oligoelements supplements were not needed to prepare the culture medium. Molasses and tuna-by-product, non-conventional substrates, can be used efficiently for BS production by A. migu...
The condensation of several primary amines and diamines with various N-ethoxycarbonyles N-tosylhy... more The condensation of several primary amines and diamines with various N-ethoxycarbonyles N-tosylhydrazonates (1a-b), triazolones (2) and bis-triazolone (3) resulted in ethanol under ultrasound irradiation. Compared with the conventional methods, the main advantages of the present procedure are milder conditions, shorter reaction time and higher yields. The newly synthesized compounds were evaluated for angiotensin I-converting enzyme (ACE) inhibition. The results were compared to Captopril as a reference drug. Compounds 3b, 2h, 3a, 2d, and 2f showed not only inhibition activity with IC values of 0.162, 0.253, 0.253, 0.281 and 0.382 µM, respectively, but also minimal toxicity. The docking of chemical compounds in the ACE active site showed possible inhibitory effect of all compounds on the catalytic activity of the enzyme, which would satisfactorily explain the anti-hypertensive effect of these compounds.
Here we report the cDNA cloning of a phospholipase A (PLA) from five Sparidae species. The deduce... more Here we report the cDNA cloning of a phospholipase A (PLA) from five Sparidae species. The deduced amino acid sequences show high similarity with pancreatic PLA. In addition, a phylogenetic tree derived from alignment of various available sequences revealed that Sparidae PLA are closer to avian PLA group IB than to mammals' ones. In order to understand the structure-function relationships of these enzymes, we report here the recombinant expression in E.coli, the refolding and characterization of His-tagged annular seabream PLA (AsPLA). A single Ni-affinity chromatography step was used to obtain a highly purified recombinant AsPLA with a molecular mass of 15kDa as attested by gel electrophoresis and MALDI-TOF mass spectrometry data. The enzyme has a specific activity of 400U.mg measured on phosphatidylcholine at pH 8.5 and 50°C. The enzyme high thermo-activity and thermo-stability make it a potential candidate in various biological applications. The 3D structure models of these enzymes were compared with structures of phylogenetically related pancreatic PLA. By following these models and utilizing molecular dynamics simulations, the resistance of the AsPLA at high temperatures was explained. Using the monomolecular film technique, AsPLA was found to be active on various phospholipids spread at the air/water interface at a surface pressure between 12 and 25dyncm. Interestingly, this enzyme was shown to be mostly active on dilauroyl-phosphatidylglycerol monolayers and this behavior was confirmed by molecular docking and dynamics simulations analysis. The discovery of a thermo-active new member of Sparidae PLA, provides new insights on structure-activity relationships of fish PLA.
International Journal of Biological Macromolecules, 2017
In order to identify fish enzymes displaying novel biochemical properties, we choose the common s... more In order to identify fish enzymes displaying novel biochemical properties, we choose the common smooth-hound (Mustelus mustelus) as a starting biological material to characterize the digestive lipid hydrolyzing enzyme. A smooth-hound digestive lipase (SmDL) was purified from a delipidated pancreatic powder. The SmDL molecular weight was around 50kDa. Specific activities of 2200 and 500U/mg were measured at pH 9 and 40°C using tributyrin and olive oil emulsion as substrates, respectively. Unlike known mammal pancreatic lipases, the SmDL was stable at 50°C and it retained 90% of its initial activity after 15min of incubation at 60°C. Interestingly, bile salts act as an activator of the SmDL. It's worth to notice that the SmDL was also salt-tolerant since it was active in the presence of high salt concentrations reaching 0.8M. Fatty acid (FA) analysis of oil from the smooth-hound viscera showed a dominance of unsaturated ones (UFAs). Interestingly, the major n-3 fatty acids were DHA and EPA with contents of 18.07% and 6.14%, respectively. In vitro digestibility model showed that the smooth hound oil was efficiently hydrolyzed by pancreatic lipases, which suggests the higher assimilation of fish oils by consumers.
Journal of agricultural and food chemistry, Jan 22, 2017
Novel phospholipase (PLA2) genes from the Sparidae family were cloned. The sequenced PLA2 reveale... more Novel phospholipase (PLA2) genes from the Sparidae family were cloned. The sequenced PLA2 revealed an identity with pancreatic PLA2 group IB. To better understand the structure/function relationships of these enzymes and their evolution, the Diplodus annularis PLA2 (DaPLA2) was overexpressed in E. coli. The refolded enzyme was purified by Ni-affinity chromatography and has a molecular mass of 15 kDa as determined by MALDI-TOF spectrometry. Interestingly, unlike the pancreatic type, the DaPLA2 was active and stable at higher temperatures, which suggests its great potential in biotechnological applications. The 3D structure of DaPLA2 was constructed to gain insights into the functional properties of sparidae PLA2. Molecular docking and dynamic simulations were performed to explain the higher thermal stability and the substrate specificity of DaPLA2. Using the monolayer technique, the purified DaPLA2 was found to be active on various phospholipids ranging from 10 to 20 mN·m(-1), which ...
ABSTRACT An esterase was purified from the golden grey mullet viscera using successively a Sephac... more ABSTRACT An esterase was purified from the golden grey mullet viscera using successively a Sephacryl S-100 gel filtration, an anion-exchange chromatography and a high-performance 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).
ABSTRACT A highly thermostable and alkaline lichenase was isolated from the newly isolated strain... more ABSTRACT A highly thermostable and alkaline lichenase was isolated from the newly isolated strain Bacillus UEB-S. A single step purification was achieved by heating the enzyme extract for 30 min at 90 °C. The enzyme was a monomeric protein with a molecular weight of 28 kDa. The optimal temperature and pH for UEB-S lichenases activity were 60 °C and 6.0, respectively. More remarkably, the purified lichenase was stable over a broad range of temperature and pH. It retained more than 60% of its activity after incubation at 90 °C for 30 min. Substrate specificity studies revealed that the enzyme is a true lichenase. A genomic library was screened. It allows the identification of a gene that encodes a putative lichenase showing 98% identity with the lichenase from Bacillus subtilis 168. Sequence comparison revealed that the two enzymes differed by two mutations at positions 69 and 83, where Val 69 and Ser 83are replaced by Met and Ala amino acids, respectively. Therefore, a theoretical structural model was built using the lichenase from Bacillus subtilis 168 Pdb code (3o5sA) structure as template. Comparison of the two 3D structures suggested that Val 69 stabilizes a calcium binding site and could be involved in the higher stability of the enzyme.
In order to identify fish enzymes displaying novel biochemical properties, we have chosen the com... more 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 %.
... In vitro, the max-155 9 Digestive Lipases Inhibition: an In vitro Study Ali Tiss, Nabil Miled... more ... In vitro, the max-155 9 Digestive Lipases Inhibition: an In vitro Study Ali Tiss, Nabil Miled, Robert Verger, Youssef Gargouri, and Abdelkarim Abousalham Lipases and Phospholipases in Drug Development: From Biochemistry to Molecular Pharmacology. ...
European Journal of Lipid Science and Technology, 2015
ABSTRACT Using lipid emulsions as well as the monomolecular film technique, we studied some kinet... more ABSTRACT Using lipid emulsions as well as the monomolecular film technique, we studied some kinetic properties of sardine digestive lipase (SaDL). The pure lipase was able to hydrolyse a triolein emulsion in the absence of any additives and seems therefore to tolerate the accumulation of long free fatty acids at the interface. The kinetic behaviour of SaDL can be explained by the high penetration capacity of this enzyme into a lipidic interface. SaDL hydrolyzes efficiently pure tributyrin, in the absence of additives. Subsequently, the sardine lipase is not denaturated at high interfacial energy. A kinetic study of the surface pressure dependency of the regioselectivity of SaDL was performed using an optically pure stereoisomer of diglyceride (1,2-sn dicaprin) and a prochiral isomer (1,3-sn-dicaprin) that were spread as monomolecular films at the air-water interface. At low surface pressure, SaDL acts preferentially on distal carboxylic ester groups of the diglyceride isomer (1,3-sn-dicaprin) but at high surface pressure, this enzyme prefers adjacent ester groups of the (1,2-sn-dicaprin) isomer. Interestingly, the sardine digestive lipase was found to hydrolyse efficiently the secondary ester group of a triglyceride analog. This is in line with the fact that SaDL hydrolysed triolein at the sn-2 position, as shown using the thin-layer chromatography technique. This property is sought for the synthesis of specific triacylglycerol-based compounds, such as structured lipids.
Abstract: Turkey pancreatic lipase immobilized on celite was used to produce fatty acids, diacylg... more Abstract: Turkey pancreatic lipase immobilized on celite was used to produce fatty acids, diacylglycerols and monoacylglycerols by hydrolysis of palm olein in a solvent free system. Turkey lipase preparation was obtained out of a delipidated pancreatic for a biotechnological application. The effect of process variables on enzymatic hydrolysis was investigated, and the maximization of hydrolysis rate was carried out using an experimental design technique. A high degree of hydrolysis (71.85±1.618%) was reached under ...
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