The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform
Moncef Nasri - One of the best experts on this subject based on the ideXlab platform.
-
Simultaneous production of alkaline amylase and biosurfactant by Bacillus methylotrophicus DCS1: application as Detergent Additive.
Biodegradation, 2018Co-Authors: Noomen Hmidet, Nawel Jemil, Moncef NasriAbstract:This study investigated the coproduction of alkaline amylase and lipopeptides by Bacillus methylotrophicus DCS1 strain, as well as their biochemical characterisation. The best production of both amylase and biosurfactant was obtained when potato starch (10 g/L) and glutamic acid (5 g/L) were used as carbon and nitrogen sources, respectively. The bacterial strain was incubated for 48 h at 25 °C and 150 rpm. This strain produced a unique amylase as showed by zymography technique. The optima pH and temperature were 60–65 °C and 8.0, respectively. Amylase activity was partially inhibited by EDTA (5 mM). The main hydrolysis products of potato starch were maltose and maltotriose. The alkaline amylase showed excellent stability and compatibility with various solid and liquid Detergents. Furthermore, the biosurfactant, produced simultaneously with alkaline amylase, demonstrated high stability at different ranges of salinity, pH, and temperature. Considering its promising properties, B. methylotrophicus DCS1 crude extract containing both biosurfactants and amylase activity may be considered as a potential candidate for future use in Detergent processing industries and environmental remediation processes.
-
Proteolytic and amylolytic enzymes from a newly isolated Bacillus mojavensis SA: Characterization and applications as laundry Detergent Additive and in leather processing.
International journal of biological macromolecules, 2017Co-Authors: Amal Hammami, Moncef Nasri, Ola Abdelhedi, Nahed Fakhfakh, Ahmed BayoudhAbstract:Abstract The present work aims to study the simultaneous production of highly alkaline proteases and thermostable α-amylases by a newly isolated bacterium Bacillus mojavensis SA. The optimum pH and temperature of amylase activity were 9.0 and 55 °C, respectively, while those of the proteolytic activity were 12.0 and 60 °C, respectively. Both α-amylase and protease enzymes showed a high stability towards a wide range of pH and temperature. Furthermore, SA crude enzymes were relatively stable towards non-ionic (Tween 20, Tween 80 and Triton X-100) and anionic (SDS) surfactants, as well as oxidizing agents. Both activities were improved by the presence of polyethylene glycol 4000 and glycerol. Additionally, the crude enzymes showed excellent stability against various solid and liquid Detergents. Wash performance analysis revealed that the SA crude enzymes exhibited a remarkable efficiency in the removal of a variety type of stains, such as blood, chocolate, coffee and oil. On the other side, SA proteases revealed a potential dehairing activity of animal hide without chemical assistance or fibrous proteins hydrolysis. Thus, considering their promising properties, B. mojavensis SA crude enzymes could be used in several biotechnological bioprocesses.
-
alkaline proteases from a newly isolated micromonospora chaiyaphumensis s103 characterization and application as a Detergent Additive and for chitin extraction from shrimp shell waste
International Journal of Biological Macromolecules, 2017Co-Authors: Samiha Mhamdi, Moncef Nasri, Naourez Ktari, Sawssen Hajji, Alya Sellami KamounAbstract:Abstract The present study was undertaken to characterize the extracellular thermostable serine alkaline proteases from newly actinomycete strain Micromonospora chaiyaphumensis S103 and to describe their evaluation in commercial Detergents and shrimp waste deproteinization. This proteolytic crude extract was active and stable in alkaline solution. It was extremely stable in the pH range of 5.0–12.0. The optimum pH and temperature were 8.0 and 70 °C, respectively, using casein as a substrate. The thermoactivity and thermostability of proteases were enhanced by the addition of 5 mM Ca2+. Proteases from S103 were also used for shrimp wastes deproteinization in the process of chitin preparation. The percent of protein removal after 3 h hydrolysis at 45 °C with an enzyme/substrate ratio of 20 U/mg had reached 93%. Furthermore, S103 crude enzyme was stable towards several organic solvents and retained 100% of its original activity after 90 days of incubation in the presence of methanol, hexane, acetone, and DMSO. These properties make S103 proteases an ideal choice for application in Detergent formulations, chitin production, and enzymatic peptide synthesis.
-
Surfactant- and oxidant-stable alkaline proteases from Bacillus invictae: Characterization and potential applications in chitin extraction and as a Detergent Additive.
International journal of biological macromolecules, 2016Co-Authors: Amal Hammami, Moncef Nasri, Marwa Hamdi, Ola Abdelhedi, Mourad Jridi, Ahmed BayoudhAbstract:A newly alkaline proteases producing strain was isolated from sea water. The strain was identified as Bacillus invictae on the basis of biochemical characteristics and 16S rRNA sequence analysis. The crude protease activity showed an optimal activity at approximately 60°C and in wide pH interval ranging from 9.0 to 11.0. At least six clear caseinolytic protease bands were observed in a zymogram. Phenylmethylsulfonyl fluoride (PMSF), a serine-protease inhibitor, was found to inhibit completely the protease activity. The crude alkaline proteases showed high stability toward solid and liquid Detergents. Furthermore, wash performance analysis revealed that the crude enzyme could effectively remove blood stain when added to commercial Detergent. In addition, the crude proteases were found to be effective in the deproteinization of shrimp shell waste. The percent of protein removal after 3h of hydrolysis at 50°C with an E/S ratio of 10U/mg of protein or after fermentation by the strain were about 76% and 82%, respectively. Thus, the results of the present study showed that the crude proteases of B. invectae could be effectively used in several industrial applications, as an eco-friendly agent.
-
New proteases extracted from red scorpionfish (Scorpaena scrofa) viscera: Characterization and application as a Detergent Additive and for shrimp waste deproteinization
Food and Bioproducts Processing, 2015Co-Authors: Islem Younes, Rim Nasri, Kemel Jellouli, Intidhar Bkhairia, Moncef NasriAbstract:Abstract Alkaline proteases from the red scorpionfish ( Scorpaena scrofa ) viscera were extracted and characterized. This proteolytic crude extract was active and stable in alkaline solution: it was extremely stable in the pH range of 5.0–12.0; the optimum pH and temperature were 10.0 and 55 °C, respectively, using casein as a substrate. Three caseinolytic proteases clear bands were observed in the zymogram test suggesting the presence of at least three different major proteinases. This proteolytic crude extract was then tested for its potential applications, especially in laundry Detergents and shrimp waste treatment. Results showed that it was extremely stable toward non-ionic surfactants (Tween 20, Tween 80 and Triton X-100). It was also stable in the presence of oxidizing agents, retaining 100% of its initial activity in the presence of 1% sodium perborate. Interestingly, it showed relative stability and compatibility with commercial liquid and solid Detergents. These properties and the high activity in high alkaline pH make these proteases an ideal choice for application in Detergent formulations. Additionally, S. scrofa proteases were found to be effective in the deproteinization of shrimp waste. A high level of deproteinization 83 ± 1.3% was recorded with an E/S ratio of 10 U/mg after 3 h incubation at 50 °C. These results suggest that enzymatic deproteinization of the shrimp waste, using S. scrofa proteases, could be applicable to the chitin production process.
Kemel Jellouli - One of the best experts on this subject based on the ideXlab platform.
-
New proteases extracted from red scorpionfish (Scorpaena scrofa) viscera: Characterization and application as a Detergent Additive and for shrimp waste deproteinization
Food and Bioproducts Processing, 2015Co-Authors: Islem Younes, Rim Nasri, Kemel Jellouli, Intidhar Bkhairia, Moncef NasriAbstract:Abstract Alkaline proteases from the red scorpionfish ( Scorpaena scrofa ) viscera were extracted and characterized. This proteolytic crude extract was active and stable in alkaline solution: it was extremely stable in the pH range of 5.0–12.0; the optimum pH and temperature were 10.0 and 55 °C, respectively, using casein as a substrate. Three caseinolytic proteases clear bands were observed in the zymogram test suggesting the presence of at least three different major proteinases. This proteolytic crude extract was then tested for its potential applications, especially in laundry Detergents and shrimp waste treatment. Results showed that it was extremely stable toward non-ionic surfactants (Tween 20, Tween 80 and Triton X-100). It was also stable in the presence of oxidizing agents, retaining 100% of its initial activity in the presence of 1% sodium perborate. Interestingly, it showed relative stability and compatibility with commercial liquid and solid Detergents. These properties and the high activity in high alkaline pH make these proteases an ideal choice for application in Detergent formulations. Additionally, S. scrofa proteases were found to be effective in the deproteinization of shrimp waste. A high level of deproteinization 83 ± 1.3% was recorded with an E/S ratio of 10 U/mg after 3 h incubation at 50 °C. These results suggest that enzymatic deproteinization of the shrimp waste, using S. scrofa proteases, could be applicable to the chitin production process.
-
Trypsin from zebra blenny (Salaria basilisca) viscera: Purification, characterisation and potential application as a Detergent Additive
Food Chemistry, 2012Co-Authors: Naourez Ktari, Kemel Jellouli, Hayet Ben Khaled, Rim Nasri, Sofiane Ghorbel, Moncef NasriAbstract:Abstract An alkaline trypsin was purified from the viscera of zebra blenny (Salaria basilisca) by ammonium sulphate (40−80% saturation) precipitation, Sephadex G-100, Mono Q-Sepharose and ultrafiltration. A yield of 12% with a purification-fold of 4.2 was obtained. The trypsin had an apparent molecular weight of 27 kDa. Soybean trypsin inhibitor and phenylmethylsulfonyl fluoride showed a strong inhibitory effect on the purified trypsin. Trypsin had maximal activity at pH 9.5 and 60 °C for the hydrolysis of Nα-benzoyl- d l -arginine-p-nitroanilide (BAPNA). It was stable at low temperatures and in the pH range of 7.0−12.0. The N-terminal amino acid sequence of the first 12 amino acids of the purified protease was IVGGRECTEPSQ. S. basilisca trypsin, which showed high homology with other fish trypsins, had a charged Arg residue at position 5, where Tyr is common in marine vertebrates and mammalian trypsins. The trypsin kinetic constants, Km and kcat for BAPNA, were 0.6 mM and 1.38 s−1, respectively.
-
Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a Detergent Additive and for shrimp waste deproteinization
Process Biochemistry, 2011Co-Authors: Kemel Jellouli, Rym Agrebi, Olfa Ghorbel-bellaaj, Hanen Ben Ayed, Laila Manni, Moncef NasriAbstract:Abstract A Detergent stable alkaline serine-protease from Bacillus licheniformis MP1 was purified in three steps: ultrafiltration using a 10 kDa cut-off membrane, Sephadex G-100 gel filtration, and Mono Q-Sepharose ion exchange chromatography with a 3.9-fold increase in specific activity and 48.2% recovery. The N-terminal amino acid sequence of the first 14 amino acids of the purified enzyme was AQTVPYGIPLIKAD. The molecular weight of the purified enzyme was estimated to be 30 kDa. The optimum pH and temperature of the purified protease were 10.0 and 70 °C, respectively, using casein as a substrate. It showed high stability towards alkaline pH, non-ionic surfactants and was relatively stable towards SDS. Additionally, the crude enzyme showed higher stability and compatibility with various laundry Detergents from Tunisian market, and the addition of MP1 proteolytic preparation (40 U/ml) to wash solution, enhance bloodstain elimination. In addition, when used in shrimp waste deproteinization at E/S = 20 U/mg protein ratio, MP1 proteolytic preparation leads to 75% deproteinization. The aprMP1 gene, encoding the alkaline protease from B. licheniformis MP1, was isolated, and its DNA sequence was determined. The deduced amino acid sequence of the preproenzyme showed high homology with many other known serine protease genes, and some differences that characterize it.
-
an oxidant and solvent stable protease produced by bacillus cereus sv1 application in the deproteinization of shrimp wastes and as a laundry Detergent Additive
Applied Biochemistry and Biotechnology, 2010Co-Authors: Laila Manni, Rym Agrebi, Alya Sellamikamoun, Anissa Haddar, Kemel Jellouli, Olfa Ghorbelbellaaj, Moncef NasriAbstract:The current increase in amount of shrimp wastes produced by the shrimp industry has led to the need in finding new methods for shrimp wastes disposal. In this study, an extracellular organic solvent- and oxidant-stable metalloprotease was produced by Bacillus cereus SV1. Maximum protease activity (5,900 U/mL) was obtained when the strain was grown in medium containing 40 g/L shrimp wastes powder as a sole carbon source. The optimum pH, optimum temperature, pH stability, and thermal stability of the crude enzyme preparation were pH 8.0, 60 °C, pH 6–9.5, and <55 °C, respectively. The crude protease was extremely stable toward several organic solvents. No loss of activity was observed even after 60 days of incubation at 30 °C in the presence of 50% (v/v) dimethyl sulfoxide and ethyl ether; the enzyme retained more than 70% of its original activity in the presence of ethanol and N,N-dimethylformamide. The protease showed high stability toward anionic (SDS) and non-ionic (Tween 80, Tween 20, and Triton X-100) surfactants. Interestingly, the activity of the enzyme was significantly enhanced by oxidizing agents. In addition, the enzyme showed excellent compatibility with some commercial liquid Detergents. The protease of B. cereus SV1, produced under the optimal culture conditions, was tested for shrimp waste deproteinization in the preparation of chitin. The protein removal with a ratio E/S of 20 was about 88%. The novelties of the SV1 protease include its high stability to organic solvents and surfactants. These unique properties make it an ideal choice for application in Detergent formulations and enzymatic peptide synthesis. In addition, the enzyme may find potential applications in the deproteinization of shrimp wastes to produce chitin.
-
An oxidant- and solvent-stable protease produced by Bacillus cereus SV1: application in the deproteinization of shrimp wastes and as a laundry Detergent Additive.
Applied biochemistry and biotechnology, 2009Co-Authors: Laila Manni, Rym Agrebi, Anissa Haddar, Kemel Jellouli, Olfa Ghorbel-bellaaj, Alya Sellami-kamoun, Moncef NasriAbstract:The current increase in amount of shrimp wastes produced by the shrimp industry has led to the need in finding new methods for shrimp wastes disposal. In this study, an extracellular organic solvent- and oxidant-stable metalloprotease was produced by Bacillus cereus SV1. Maximum protease activity (5,900 U/mL) was obtained when the strain was grown in medium containing 40 g/L shrimp wastes powder as a sole carbon source. The optimum pH, optimum temperature, pH stability, and thermal stability of the crude enzyme preparation were pH 8.0, 60 degrees C, pH 6-9.5, and
Emine Atakisi - One of the best experts on this subject based on the ideXlab platform.
-
A novel Detergent Additive: Organic solvent- and thermo-alkaline-stable recombinant subtilisin.
International journal of biological macromolecules, 2017Co-Authors: Canan Gulmez, Onur Atakisi, Kezban Yildiz Dalginli, Emine AtakisiAbstract:Abstract In the present work, subtilisin gene from Bacillus subtilis PTTC 1023 was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin was purified in a single-step procedure by affinity chromatography. The molecular mass of the purified protein was determined to be about 40 kDa by SDS-PAGE. The optimum pH and temperature values of its proteolytic activity were 10.5 and 50 °C, respectively and retained more than 70% and 89% of its activity in pH range of 7–12 and 30–60 °C, respectively. Enzyme purity was estimated to be about 200- fold greater than that of the crude extract and subtilisin had a specific activity of 56.16 U/mg, with a yield of about 87.9%. It was completely inhibited by phenylmethanesulfonyl fluoride, which strongly suggests its belonging to serine protease family. Interestingly, subtilisin protease displayed a significant compatibility with commercial Detergents, and tolerance organic solvents, metallic ions and surfactants. The findings obtained demonstrated that protease of B. subtilis could potentially be used in future applications as an Additive in Detergent formulations.
-
Organic solvent stable and thermo-alkaline recombinant subtilisin as a novel biocatalytic Detergent Additive
International Journal of Biological Macromolecules, 2017Co-Authors: Canan Gulmez, Onur Atakisi, Kezban Yildiz Dalginli, Emine AtakisiAbstract:Subtilisins are serine alkaline proteases produced by Bacillus species. For the personal care industry, thermo-active and stable under alkaline conditions protease variants are of especial interest for Detergent formulations. In the present work, subtilisin gene from Bacillus subtilis PTTC 1023 was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin was purified in a single-step procedure by affinity chromatography. The molecular mass of the purified protein was determined to be about 40kDa by SDS-PAGE. The optimum pH and temperature values of its proteolytic activity were 10.5 and 50°C, respectively and retained more than 70% and 89% of its activity in pH range of 7–12 and 30–60°C, respectively. Enzyme purity was estimated to be about 200- fold greater than that of the crude extract and subtilisin had a specific activity of 56.16U/mg, with a yield of about 87.9%. It was completely inhibited by phenylmethanesulfonyl fluoride, which strongly suggests its belonging to serine protease family. Interestingly, subtilisin protease displayed a significant compatibility with commercial Detergents, and tolerance organic solvent, metal ion and surfactant. The findings obtained demonstrated that protease of B.subtilis could potentially be used in future applications as an Additive in Detergent formulations.
Canan Gulmez - One of the best experts on this subject based on the ideXlab platform.
-
Proteinase K hybrid nanoflowers (P-hNFs) as a novel nanobiocatalytic Detergent Additive
International journal of biological macromolecules, 2018Co-Authors: Canan Gulmez, Cevahir Altinkaynak, Nalan Özdemir, Onur AtakisiAbstract:In this study, enzyme-inorganic hybrid nanoflowers were synthesized using proteinase K and Cu2+ ions. The synthesized proteinase K-Cu2+ hybrid nanoflowers (P-hNFs) were characterized by their morphology and chemical point of view by using different techniques such as SEM, FTIR, EDX, and XRD. The proteolytic activities and some important characteristics such as optimum pH and temperature of the P-hNFs were also evaluated by comparison with free proteinase K. Optimum pH values of free proteinase K and P-hNFs were determined as pH 10 and pH 11, respectively. Optimum temperatures recorded for both free proteinase K (at pH 10) and P-hNFs (at pH 11) were 40 °C. In our study, for the first time, using some commercial Detergents and surfactants, the utility of the P-hNFs as a Detergent Additive was also systematically evaluated. In these studies, the P-hNFs exhibited better activity than free proteinase K in the presence of all surfactants (CHAPS, DOC, SDS, Triton X-100 and Tergitol) except for Tween 80. Importantly, the P-hNFs was more stable and compatible with all tested solid laundry Detergents. The findings demonstrated that the P-hNFs could potentially be used as an Additive in Detergent formulations.
-
A novel Detergent Additive: Organic solvent- and thermo-alkaline-stable recombinant subtilisin.
International journal of biological macromolecules, 2017Co-Authors: Canan Gulmez, Onur Atakisi, Kezban Yildiz Dalginli, Emine AtakisiAbstract:Abstract In the present work, subtilisin gene from Bacillus subtilis PTTC 1023 was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin was purified in a single-step procedure by affinity chromatography. The molecular mass of the purified protein was determined to be about 40 kDa by SDS-PAGE. The optimum pH and temperature values of its proteolytic activity were 10.5 and 50 °C, respectively and retained more than 70% and 89% of its activity in pH range of 7–12 and 30–60 °C, respectively. Enzyme purity was estimated to be about 200- fold greater than that of the crude extract and subtilisin had a specific activity of 56.16 U/mg, with a yield of about 87.9%. It was completely inhibited by phenylmethanesulfonyl fluoride, which strongly suggests its belonging to serine protease family. Interestingly, subtilisin protease displayed a significant compatibility with commercial Detergents, and tolerance organic solvents, metallic ions and surfactants. The findings obtained demonstrated that protease of B. subtilis could potentially be used in future applications as an Additive in Detergent formulations.
-
Organic solvent stable and thermo-alkaline recombinant subtilisin as a novel biocatalytic Detergent Additive
International Journal of Biological Macromolecules, 2017Co-Authors: Canan Gulmez, Onur Atakisi, Kezban Yildiz Dalginli, Emine AtakisiAbstract:Subtilisins are serine alkaline proteases produced by Bacillus species. For the personal care industry, thermo-active and stable under alkaline conditions protease variants are of especial interest for Detergent formulations. In the present work, subtilisin gene from Bacillus subtilis PTTC 1023 was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin was purified in a single-step procedure by affinity chromatography. The molecular mass of the purified protein was determined to be about 40kDa by SDS-PAGE. The optimum pH and temperature values of its proteolytic activity were 10.5 and 50°C, respectively and retained more than 70% and 89% of its activity in pH range of 7–12 and 30–60°C, respectively. Enzyme purity was estimated to be about 200- fold greater than that of the crude extract and subtilisin had a specific activity of 56.16U/mg, with a yield of about 87.9%. It was completely inhibited by phenylmethanesulfonyl fluoride, which strongly suggests its belonging to serine protease family. Interestingly, subtilisin protease displayed a significant compatibility with commercial Detergents, and tolerance organic solvent, metal ion and surfactant. The findings obtained demonstrated that protease of B.subtilis could potentially be used in future applications as an Additive in Detergent formulations.
Rym Agrebi - One of the best experts on this subject based on the ideXlab platform.
-
Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a Detergent Additive and for shrimp waste deproteinization
Process Biochemistry, 2011Co-Authors: Kemel Jellouli, Rym Agrebi, Olfa Ghorbel-bellaaj, Hanen Ben Ayed, Laila Manni, Moncef NasriAbstract:Abstract A Detergent stable alkaline serine-protease from Bacillus licheniformis MP1 was purified in three steps: ultrafiltration using a 10 kDa cut-off membrane, Sephadex G-100 gel filtration, and Mono Q-Sepharose ion exchange chromatography with a 3.9-fold increase in specific activity and 48.2% recovery. The N-terminal amino acid sequence of the first 14 amino acids of the purified enzyme was AQTVPYGIPLIKAD. The molecular weight of the purified enzyme was estimated to be 30 kDa. The optimum pH and temperature of the purified protease were 10.0 and 70 °C, respectively, using casein as a substrate. It showed high stability towards alkaline pH, non-ionic surfactants and was relatively stable towards SDS. Additionally, the crude enzyme showed higher stability and compatibility with various laundry Detergents from Tunisian market, and the addition of MP1 proteolytic preparation (40 U/ml) to wash solution, enhance bloodstain elimination. In addition, when used in shrimp waste deproteinization at E/S = 20 U/mg protein ratio, MP1 proteolytic preparation leads to 75% deproteinization. The aprMP1 gene, encoding the alkaline protease from B. licheniformis MP1, was isolated, and its DNA sequence was determined. The deduced amino acid sequence of the preproenzyme showed high homology with many other known serine protease genes, and some differences that characterize it.
-
an oxidant and solvent stable protease produced by bacillus cereus sv1 application in the deproteinization of shrimp wastes and as a laundry Detergent Additive
Applied Biochemistry and Biotechnology, 2010Co-Authors: Laila Manni, Rym Agrebi, Alya Sellamikamoun, Anissa Haddar, Kemel Jellouli, Olfa Ghorbelbellaaj, Moncef NasriAbstract:The current increase in amount of shrimp wastes produced by the shrimp industry has led to the need in finding new methods for shrimp wastes disposal. In this study, an extracellular organic solvent- and oxidant-stable metalloprotease was produced by Bacillus cereus SV1. Maximum protease activity (5,900 U/mL) was obtained when the strain was grown in medium containing 40 g/L shrimp wastes powder as a sole carbon source. The optimum pH, optimum temperature, pH stability, and thermal stability of the crude enzyme preparation were pH 8.0, 60 °C, pH 6–9.5, and <55 °C, respectively. The crude protease was extremely stable toward several organic solvents. No loss of activity was observed even after 60 days of incubation at 30 °C in the presence of 50% (v/v) dimethyl sulfoxide and ethyl ether; the enzyme retained more than 70% of its original activity in the presence of ethanol and N,N-dimethylformamide. The protease showed high stability toward anionic (SDS) and non-ionic (Tween 80, Tween 20, and Triton X-100) surfactants. Interestingly, the activity of the enzyme was significantly enhanced by oxidizing agents. In addition, the enzyme showed excellent compatibility with some commercial liquid Detergents. The protease of B. cereus SV1, produced under the optimal culture conditions, was tested for shrimp waste deproteinization in the preparation of chitin. The protein removal with a ratio E/S of 20 was about 88%. The novelties of the SV1 protease include its high stability to organic solvents and surfactants. These unique properties make it an ideal choice for application in Detergent formulations and enzymatic peptide synthesis. In addition, the enzyme may find potential applications in the deproteinization of shrimp wastes to produce chitin.
-
An oxidant- and solvent-stable protease produced by Bacillus cereus SV1: application in the deproteinization of shrimp wastes and as a laundry Detergent Additive.
Applied biochemistry and biotechnology, 2009Co-Authors: Laila Manni, Rym Agrebi, Anissa Haddar, Kemel Jellouli, Olfa Ghorbel-bellaaj, Alya Sellami-kamoun, Moncef NasriAbstract:The current increase in amount of shrimp wastes produced by the shrimp industry has led to the need in finding new methods for shrimp wastes disposal. In this study, an extracellular organic solvent- and oxidant-stable metalloprotease was produced by Bacillus cereus SV1. Maximum protease activity (5,900 U/mL) was obtained when the strain was grown in medium containing 40 g/L shrimp wastes powder as a sole carbon source. The optimum pH, optimum temperature, pH stability, and thermal stability of the crude enzyme preparation were pH 8.0, 60 degrees C, pH 6-9.5, and
-
two Detergent stable alkaline serine proteases from bacillus mojavensis a21 purification characterization and potential application as a laundry Detergent Additive
Bioresource Technology, 2009Co-Authors: Anissa Haddar, Rym Agrebi, Ali Bougatef, Alya Sellamikamoun, Noomen Hmidet, Moncef NasriAbstract:Abstract Two Detergent stable alkaline serine-proteases (BM1 and BM2) from Bacillus mojavensis A21 were purified. The molecular weights of BM1 and BM2 enzymes determined by SDS–PAGE were approximately 29,000 Da and 15,500 Da, respectively. The optimum pH values of BM1 and BM2 proteases were shown to be 8.0–10.0 and 10.0, respectively. Both enzymes exhibited maximal activity at 60 °C, using casein as a substrate. The N-terminal amino acid sequences of BM1 and BM2 proteases were AQSVPYGISQIKA and AIPDQAATTLL , respectively. Both proteases showed high stability towards non-ionic surfactants. The enzymes were found to be relatively stable towards oxidizing agents. In addition, both enzymes showed excellent stability and compatibility with a wide range of commercial liquid and solid Detergents. These properties and the high activity in high alkaline pH make these proteases an ideal choice for application in Detergent formulations.