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Ana Lúcia Figueiredo Porto - One of the best experts on this subject based on the ideXlab platform.
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Single step purification via magnetic nanoparticles of new broad pH active protease from Penicillium aurantiogriseum
Protein expression and purification, 2018Co-Authors: José Manoel Wanderley Duarte Neto, Carolina De Albuquerque Lima, Maria Carolina De Albuquerque Wanderley, Ana Lúcia Figueiredo PortoAbstract:Abstract A new set of applications can be achieved when using high stability proteases. Industrially, high costs can be related to production medium and purification process. Magnetic nanoparticles have been successfully used for rapid and scalable purification. In this work, azocasein were immobilized on magnetite nanoparticles and applied in a single step purification of protease produced by Penicillium aurantiogriseum using soybean flour medium, and the new purified enzyme was characterized. Glutaraldehyde activated nanoparticles were used in azocasein immobilization and then incubated with dialyzed 60–80% saline precipitation fraction of crude extract for purification. Adsorbents were washed 7 times (0.1 M NaCl solution) and eluted 3 times (1 M NaCl solution), these final elutions contained the purified protease. This protease was purified 55.68-fold, retaining 46% of its original activity. Presented approximately 40 kDa on SDS-PAGE and optimum activity at 45 °C and pH 9.0. Maintained over 60% of activity from pH 6.0 to 11.0. Kept more than 50% activity from 15 to 55 °C, did not lose any activity over 48 h at 25 °C. Inhibitors assay suggested a serine protease with aspartic residues on its active site. Results report a successful application of an alternative purification method and novel broad pH tolerant protease.
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Optimization of Penicillium aurantiogriseum protease immobilization on magnetic nanoparticles for antioxidant peptides’ obtainment
Preparative biochemistry & biotechnology, 2017Co-Authors: José Manoel Wanderley Duarte Neto, Carolina De Albuquerque Lima, Daniela De Araújo Viana Marques, J. C. Maciel, Júlia Furtado Campos, Luiz Bezerra De Carvalho Júnior, Ana Lúcia Figueiredo PortoAbstract:ABSTRACTThis work reports an optimization of protease from Penicillium aurantiogriseum immobilization on polyaniline-coated magnetic nanoparticles for antioxidant peptides’ obtainment derived from bovine casein. Immobilization process was optimized using a full two-level factorial design (24) followed by a response surface methodology. Using the derivative, casein was hydrolyzed uncovering its peptides that were sequenced and had antioxidant properties tested through (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt) (ABTS) radical scavenging and hydrogen peroxide scavenging assays. Optimal conditions for immobilization were 2 hr of immobilization, offered protein amount of 200 µg/mL, immobilization pH of 6.3 and 7.3 hr of activation. Derivative keeps over 74% of its original activity after reused five times. Free and immobilized enzyme casein hydrolysates presented similar peptide mass fingerprints, and prevalent peptides could be sequenced. Hydrolysates presented more than 2.5× hig...
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Production of antioxidant hydrolysate from bovine casein using immobilized Penicillium aurantiogriseum protease on magnetic nanoparticles
2014Co-Authors: Ana Lúcia Figueiredo Porto, José Manoel Wanderley Duarte Neto, J. C. Maciel, Luiz Bezerra De Carvalho Júnior, Carolina De Albuquerque LimaAbstract:Peptides with bioactive properties can be released from the precursor proteins during food processing or digestion, and act as antioxidative compounds. Although, it has been proven that hydrolysate exerts higher antioxidant activity than purified peptides. The process of enzyme immobilization proved to be more practical and advantageous for catalysis than using free enzyme. The aim of this study was to use a protease produced by Penicillium aurantiogriseum immobilized on polianilin-coated magnetic nanoparticles, for bovine casein hydrolysis and to evaluate the hydrolysate antioxidant properties. The 60-80% saline fraction of crude extract was used in immobilization. Commercial casein from bovine milk 1% (w/v) was hydrolyzed by 10 mg/mL of immobilized protease. The casein hydrolysates were used in ABTS and H2O2 scavenging activity assays, where Trolox was used as standard. In the ABTS scavenging assay, the hydrolysate (1% w/v) revealed a 1341 μmol of Trolox equivalent activity and in the hydrogen peroxide scavenging assay, the hydrolysate (using 0.1% w/v) presented a 547.82 μmol of Trolox equivalent activity. In both assays the hydrolysates presented a more than 2.5 times greater activity than non-hydrolyzed casein, which validates the process capacity of developing casein derived natural antioxidant ingredients with potential for functional foods.
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Two-phase partitioning and partial characterization of a collagenase from Penicillium aurantiogriseum URM4622: Application to collagen hydrolysis
Biochemical Engineering Journal, 2013Co-Authors: Carolina De Albuquerque Lima, José Luiz De Lima Filho, Daniela De Araújo Viana Marques, Maria G. Carneiro-da-cunha, Attilio Converti, Augusto Cézar Vasconcelos De Freitas Júnior, Ana Lúcia Figueiredo PortoAbstract:Abstract Aqueous two-phase systems (ATPS) of PEG/phosphate were used to recover collagenase from Penicillium aurantiogriseum from fermented broth. Experiments were carried out according to a 2 4 -full factorial design using the PEG molar mass ( M PEG ), PEG concentration ( C PEG ), phosphate concentration ( C PHOS ) and pH as the independent variables, and the purification factor ( PF ), partition coefficient ( K ) and activity yield ( Y ) as the responses. All the responses increased in the top phase with increasing C PEG and C PHOS and decreasing M PEG , but the maximum value of PF (5.23) was obtained at the lowest pH (6.0), that of Y (61.68%) and K (1.52) at the highest one (8.0). The electrophoretic profile revealed that some protein contaminants were removed by the ATPS, and the extracted collagenase exhibited optimum activity at pH 8.0 and 45 °C. The proposed ATPS appears to be a promising alternative to conventional first-step operations for direct recovery of collagenase from fermented broths, yielding a concentrate enzyme solution able to effectively hydrolyze collagen.
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Partitioning and extraction of collagenase from Penicillium aurantiogriseum in poly(ethylene glycol)/phosphate aqueous two-phase system
Fluid Phase Equilibria, 2012Co-Authors: Bruno Ubertino Rosso, Carolina De Albuquerque Lima, Maria G. Carneiro-da-cunha, Attilio Converti, Tatiana Souza Porto, Cynthia O. Nascimento, Adalberto Pessoa Junior, Ana Lúcia Figueiredo PortoAbstract:Abstract Purification of collagenase produced by Penicillium aurantiogriseum URM4622 was carried using a PEG/phosphate aqueous two-phase system (ATPS). A 2 3 -full experimental design was used to investigate the influence of PEG molar mass, PEG concentration and phosphate concentration on the selected responses, namely partition coefficient, activity yield and purification factor. The ATPS was composed of PEG (molar mass of 550, 1500 and 4000 g/mol) at concentrations of 15.0, 17.5 and 20.0% (w/w) and phosphate at concentrations of 12.5, 15.0 and 17.5% (w/w). The best results of one-step extraction of collagenase from the fermentation broth (partition coefficient of 1.01, activity yield of 242% and purification factor of 23.5) were obtained at pH 6.0 using 20.0% (w/w) PEG 550 and 17.5% (w/w) phosphate. The results of this preliminary study demonstrate that the selected ATPS is satisfactorily selective for the extraction of such a collagenase.
Attilio Converti - One of the best experts on this subject based on the ideXlab platform.
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Antimicrobial and radical scavenging properties of bovine collagen hydrolysates produced by Penicillium aurantiogriseum URM 4622 collagenase
Journal of Food Science and Technology, 2015Co-Authors: Carolina A. Lima, Júlia Furtado Campos, José L. Lima Filho, Attilio Converti, Maria G. Carneiro Cunha, Ana L. F. PortoAbstract:A 2^3 full factorial design was used to identify the main effects and interactions of pH, collagen concentration and temperature on the degree of collagen hydrolysis (DH) by collagenase from Penicillium aurantiogriseum URM 4622. Increases in both pH and collagen concentration improved DH, and a positive interaction effect was observed for these variables. On the other hand, temperature had a negative main effect on DH. The maximum value of DH (4.65 μg/mL) was achieved at 7.5 mg/mL collagen concentration, pH 8.0 and 25 °C. The peptide profile showed several peptides with molecular weights lower than 2 kDa and exhibited antibacterial activity against Escherichia coli , Bacillus subtilis and Staphylococcus aureus . An antioxidant activity of 84.7 ± 0.24 % towards the radical ABTS• + was obtained with 50 mg/mL hydrolysates. This study demonstrated that collagen hydrolysed by P. aurantiogriseum URM 4622 collagenase possesses interesting antibacterial and antioxidant activities.
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Two-phase partitioning and partial characterization of a collagenase from Penicillium aurantiogriseum URM4622: Application to collagen hydrolysis
Biochemical Engineering Journal, 2013Co-Authors: Carolina De Albuquerque Lima, José Luiz De Lima Filho, Daniela De Araújo Viana Marques, Maria G. Carneiro-da-cunha, Attilio Converti, Augusto Cézar Vasconcelos De Freitas Júnior, Ana Lúcia Figueiredo PortoAbstract:Abstract Aqueous two-phase systems (ATPS) of PEG/phosphate were used to recover collagenase from Penicillium aurantiogriseum from fermented broth. Experiments were carried out according to a 2 4 -full factorial design using the PEG molar mass ( M PEG ), PEG concentration ( C PEG ), phosphate concentration ( C PHOS ) and pH as the independent variables, and the purification factor ( PF ), partition coefficient ( K ) and activity yield ( Y ) as the responses. All the responses increased in the top phase with increasing C PEG and C PHOS and decreasing M PEG , but the maximum value of PF (5.23) was obtained at the lowest pH (6.0), that of Y (61.68%) and K (1.52) at the highest one (8.0). The electrophoretic profile revealed that some protein contaminants were removed by the ATPS, and the extracted collagenase exhibited optimum activity at pH 8.0 and 45 °C. The proposed ATPS appears to be a promising alternative to conventional first-step operations for direct recovery of collagenase from fermented broths, yielding a concentrate enzyme solution able to effectively hydrolyze collagen.
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Partitioning and extraction of collagenase from Penicillium aurantiogriseum in poly(ethylene glycol)/phosphate aqueous two-phase system
Fluid Phase Equilibria, 2012Co-Authors: Bruno Ubertino Rosso, Carolina De Albuquerque Lima, Maria G. Carneiro-da-cunha, Attilio Converti, Tatiana Souza Porto, Cynthia O. Nascimento, Adalberto Pessoa Junior, Ana Lúcia Figueiredo PortoAbstract:Abstract Purification of collagenase produced by Penicillium aurantiogriseum URM4622 was carried using a PEG/phosphate aqueous two-phase system (ATPS). A 2 3 -full experimental design was used to investigate the influence of PEG molar mass, PEG concentration and phosphate concentration on the selected responses, namely partition coefficient, activity yield and purification factor. The ATPS was composed of PEG (molar mass of 550, 1500 and 4000 g/mol) at concentrations of 15.0, 17.5 and 20.0% (w/w) and phosphate at concentrations of 12.5, 15.0 and 17.5% (w/w). The best results of one-step extraction of collagenase from the fermentation broth (partition coefficient of 1.01, activity yield of 242% and purification factor of 23.5) were obtained at pH 6.0 using 20.0% (w/w) PEG 550 and 17.5% (w/w) phosphate. The results of this preliminary study demonstrate that the selected ATPS is satisfactorily selective for the extraction of such a collagenase.
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Production and characterization of a collagenolytic serine proteinase by Penicillium aurantiogriseum URM 4622: A factorial study
Biotechnology and Bioprocess Engineering, 2011Co-Authors: Carolina A. Lima, Maria G. Carneiro-da-cunha, José L. Lima Filho, Attilio Converti, Benício B. Neto, Ana L. F. PortoAbstract:A 2^4 full factorial design was used to identify the main effects and interactions of the initial medium pH, soybean flour concentration, temperature and orbital agitation speed on extracellular collagenase production by Penicillium aurantiogriseum URM4622. The most significant variables for collagenase production were soybean flour concentration and initial medium pH that had positive main effects, and temperature that had a negative one. Protein concentration in soybean flour revealed to be a significant factor for the production of a collagenase serine proteinase. The most favorable production conditions were found to be 0.75% soybean flour, pH 8.0, 200 rpm, and 28°C, which led to a collagenase activity of 164 U. The enzyme showed an optimum activity at 37°C and pH 9.0, was stable over wide ranges of pH and temperature (6.0 ∼ 10.0 and 25 ∼ 45°C, respectively) and was strongly inhibited by 10 mM phenylmethylsulphonylfluoride. The firstorder rate constants for collagenase inactivation in the crude extract, calculated from semi-log plots of the residual activity versus time, were used in Arrhenius and Eyring plots to estimate the main thermodynamic parameters of thermoinactivation ( E *_ d = 107.4 kJ/mol and ΔH*_ d = 104.7 kJ/mol). The enzyme is probably an extracellular neutral serine collagenase effective on azocoll, gelatin and collagen decomposition.
Carolina De Albuquerque Lima - One of the best experts on this subject based on the ideXlab platform.
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Single step purification via magnetic nanoparticles of new broad pH active protease from Penicillium aurantiogriseum
Protein expression and purification, 2018Co-Authors: José Manoel Wanderley Duarte Neto, Carolina De Albuquerque Lima, Maria Carolina De Albuquerque Wanderley, Ana Lúcia Figueiredo PortoAbstract:Abstract A new set of applications can be achieved when using high stability proteases. Industrially, high costs can be related to production medium and purification process. Magnetic nanoparticles have been successfully used for rapid and scalable purification. In this work, azocasein were immobilized on magnetite nanoparticles and applied in a single step purification of protease produced by Penicillium aurantiogriseum using soybean flour medium, and the new purified enzyme was characterized. Glutaraldehyde activated nanoparticles were used in azocasein immobilization and then incubated with dialyzed 60–80% saline precipitation fraction of crude extract for purification. Adsorbents were washed 7 times (0.1 M NaCl solution) and eluted 3 times (1 M NaCl solution), these final elutions contained the purified protease. This protease was purified 55.68-fold, retaining 46% of its original activity. Presented approximately 40 kDa on SDS-PAGE and optimum activity at 45 °C and pH 9.0. Maintained over 60% of activity from pH 6.0 to 11.0. Kept more than 50% activity from 15 to 55 °C, did not lose any activity over 48 h at 25 °C. Inhibitors assay suggested a serine protease with aspartic residues on its active site. Results report a successful application of an alternative purification method and novel broad pH tolerant protease.
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Optimization of Penicillium aurantiogriseum protease immobilization on magnetic nanoparticles for antioxidant peptides’ obtainment
Preparative biochemistry & biotechnology, 2017Co-Authors: José Manoel Wanderley Duarte Neto, Carolina De Albuquerque Lima, Daniela De Araújo Viana Marques, J. C. Maciel, Júlia Furtado Campos, Luiz Bezerra De Carvalho Júnior, Ana Lúcia Figueiredo PortoAbstract:ABSTRACTThis work reports an optimization of protease from Penicillium aurantiogriseum immobilization on polyaniline-coated magnetic nanoparticles for antioxidant peptides’ obtainment derived from bovine casein. Immobilization process was optimized using a full two-level factorial design (24) followed by a response surface methodology. Using the derivative, casein was hydrolyzed uncovering its peptides that were sequenced and had antioxidant properties tested through (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt) (ABTS) radical scavenging and hydrogen peroxide scavenging assays. Optimal conditions for immobilization were 2 hr of immobilization, offered protein amount of 200 µg/mL, immobilization pH of 6.3 and 7.3 hr of activation. Derivative keeps over 74% of its original activity after reused five times. Free and immobilized enzyme casein hydrolysates presented similar peptide mass fingerprints, and prevalent peptides could be sequenced. Hydrolysates presented more than 2.5× hig...
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Production of antioxidant hydrolysate from bovine casein using immobilized Penicillium aurantiogriseum protease on magnetic nanoparticles
2014Co-Authors: Ana Lúcia Figueiredo Porto, José Manoel Wanderley Duarte Neto, J. C. Maciel, Luiz Bezerra De Carvalho Júnior, Carolina De Albuquerque LimaAbstract:Peptides with bioactive properties can be released from the precursor proteins during food processing or digestion, and act as antioxidative compounds. Although, it has been proven that hydrolysate exerts higher antioxidant activity than purified peptides. The process of enzyme immobilization proved to be more practical and advantageous for catalysis than using free enzyme. The aim of this study was to use a protease produced by Penicillium aurantiogriseum immobilized on polianilin-coated magnetic nanoparticles, for bovine casein hydrolysis and to evaluate the hydrolysate antioxidant properties. The 60-80% saline fraction of crude extract was used in immobilization. Commercial casein from bovine milk 1% (w/v) was hydrolyzed by 10 mg/mL of immobilized protease. The casein hydrolysates were used in ABTS and H2O2 scavenging activity assays, where Trolox was used as standard. In the ABTS scavenging assay, the hydrolysate (1% w/v) revealed a 1341 μmol of Trolox equivalent activity and in the hydrogen peroxide scavenging assay, the hydrolysate (using 0.1% w/v) presented a 547.82 μmol of Trolox equivalent activity. In both assays the hydrolysates presented a more than 2.5 times greater activity than non-hydrolyzed casein, which validates the process capacity of developing casein derived natural antioxidant ingredients with potential for functional foods.
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Two-phase partitioning and partial characterization of a collagenase from Penicillium aurantiogriseum URM4622: Application to collagen hydrolysis
Biochemical Engineering Journal, 2013Co-Authors: Carolina De Albuquerque Lima, José Luiz De Lima Filho, Daniela De Araújo Viana Marques, Maria G. Carneiro-da-cunha, Attilio Converti, Augusto Cézar Vasconcelos De Freitas Júnior, Ana Lúcia Figueiredo PortoAbstract:Abstract Aqueous two-phase systems (ATPS) of PEG/phosphate were used to recover collagenase from Penicillium aurantiogriseum from fermented broth. Experiments were carried out according to a 2 4 -full factorial design using the PEG molar mass ( M PEG ), PEG concentration ( C PEG ), phosphate concentration ( C PHOS ) and pH as the independent variables, and the purification factor ( PF ), partition coefficient ( K ) and activity yield ( Y ) as the responses. All the responses increased in the top phase with increasing C PEG and C PHOS and decreasing M PEG , but the maximum value of PF (5.23) was obtained at the lowest pH (6.0), that of Y (61.68%) and K (1.52) at the highest one (8.0). The electrophoretic profile revealed that some protein contaminants were removed by the ATPS, and the extracted collagenase exhibited optimum activity at pH 8.0 and 45 °C. The proposed ATPS appears to be a promising alternative to conventional first-step operations for direct recovery of collagenase from fermented broths, yielding a concentrate enzyme solution able to effectively hydrolyze collagen.
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Partitioning and extraction of collagenase from Penicillium aurantiogriseum in poly(ethylene glycol)/phosphate aqueous two-phase system
Fluid Phase Equilibria, 2012Co-Authors: Bruno Ubertino Rosso, Carolina De Albuquerque Lima, Maria G. Carneiro-da-cunha, Attilio Converti, Tatiana Souza Porto, Cynthia O. Nascimento, Adalberto Pessoa Junior, Ana Lúcia Figueiredo PortoAbstract:Abstract Purification of collagenase produced by Penicillium aurantiogriseum URM4622 was carried using a PEG/phosphate aqueous two-phase system (ATPS). A 2 3 -full experimental design was used to investigate the influence of PEG molar mass, PEG concentration and phosphate concentration on the selected responses, namely partition coefficient, activity yield and purification factor. The ATPS was composed of PEG (molar mass of 550, 1500 and 4000 g/mol) at concentrations of 15.0, 17.5 and 20.0% (w/w) and phosphate at concentrations of 12.5, 15.0 and 17.5% (w/w). The best results of one-step extraction of collagenase from the fermentation broth (partition coefficient of 1.01, activity yield of 242% and purification factor of 23.5) were obtained at pH 6.0 using 20.0% (w/w) PEG 550 and 17.5% (w/w) phosphate. The results of this preliminary study demonstrate that the selected ATPS is satisfactorily selective for the extraction of such a collagenase.
J A Ordonez - One of the best experts on this subject based on the ideXlab platform.
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Volatile compound generation in dry fermented sausages by the surface inoculation of selected mould species
European Food Research and Technology, 2005Co-Authors: Eva Hierro, Jose M Bruna, J A Ordonez, Manuela FernandezAbstract:The effect of the inoculation of dry fermented sausage surface with an atoxigenic, proteolytic and lipolytic strain of Mucor racemosus , Penicillium aurantiogriseum and Penicillium camemberti on the volatile composition was studied. The analysis of the headspace volatile compounds using gas chromatography/mass spectrometry enabled the identification of 55 volatiles. The study showed that every mould species produced a different volatile profile which was also different from that of the control sausages. Compounds derived from amino acid catabolism, i.e. branched aldehydes and the corresponding alcohols, were produced in higher amounts in sausages inoculated with Penicillium spp. On the other hand, volatiles coming from the microbial esterification were related to sausages inoculated with M. racemosus . The development of the fungal mycelia on the sausage surface protected lipids from oxidation, thus giving rise to fewer lipid oxidation products in the inoculated sausages.
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Microbial and physico-chemical changes during the ripening of dry fermented sausages superficially inoculated with or having added an intracellular cell-free extract of Penicillium aurantiogriseum.
Meat science, 2001Co-Authors: Jose M Bruna, J A Ordonez, Manuela Fernandez, Beatriz Herranz, Lorenzo De La HozAbstract:Abstract The effect of inoculation of the “salchichon” (dry fermented sausage) surface with an atoxygenic, proteolytic and lipolytic strain of Penicillium aurantiogriseum and/or the addition of an intracellular cell-free-extract (ICFE) of the same mould on the ripening process was studied. Four batches of salchichon were manufactured: control, superficially inoculated, added with the intracellular cell free extract and combination of both treatments. Superficial mould modified Micrococcaceae counts, pH, free amino acids, lipid fractions, TBARS and some organic acids. The ICFE degraded free amino acids, producing a rise in ammonia. Both treatments combined accelerate the proteolysis and lipolysis of the sausages and also the further amino acid degradation.
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The contribution of Penicillium aurantiogriseum to the volatile composition and sensory quality of dry fermented sausages.
Meat science, 2001Co-Authors: Jose M Bruna, Eva Hierro, Manuela Fernandez, Lorenzo De La Hoz, Donald S. Mottram, J A OrdonezAbstract:An atoxygenic, proteolytic and lipolytic strain of Penicillium aurantiogriseum was tested for its ability to accelerate the production of volatile compounds and to improve the sensory properties of dry fermented sausages. The following batches of sausages were prepared: control; superficially inoculated with a spore suspension; added with an intracellular cell free extract; and superficially inoculated and added with the intracellular cell free extract. Higher levels of lipid oxidation products were found in the aroma extracts of sausages without a mould cover. In contrast, branched aldehydes and alcohols presented higher concentrations in superficially inoculated and extract added sausages, while esters only showed higher concentration in the first ones. The sensory analysis showed that sausages prepared with both treatments received the highest scores in all the properties evaluated, which demonstrated both the potential of this mould as producer of volatile compounds and the effectiveness of combining both treatments.
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combined use of pronase e and a fungal extract Penicillium aurantiogriseum to potentiate the sensory characteristics of dry fermented sausages
Meat Science, 2000Co-Authors: Jose M Bruna, Eva Hierro, Manuela Fernandez, J A OrdonezAbstract:Abstract A combination of an extract of Penicillium aurantiogriseum and Pronase E was used in an attempt to enhance the sensory characteristics of dry fermented sausages, specifically, a salami-like one named “salchichon”. The addition of Pronase E alone (600 units/kg) produced a rise in free amino acids and biogenic amines and also an increase in the ammonia content. Addition of the protease and fungal extract (100.87 mg protein/kg of mixture) brought about a decrease in the level of free amino acids and a larger increase in the ammonia content than the batch added with only Pronase E. There was also an increase in the amount of specific volatile compounds such as 2- and 3-methylbutanal, 2- and 3-methylpropanal and 2- and 3-methyl-1-butanol produced by the breakdown of amino acids in these fermented sausages. Values of pH, a w and dry matter were not affected by addition of the protease or fungal extract. In contrast, addition of Pronase E produced a notable change in the textural characteristics, reducing the hardness, cohesiveness, gumminess, chewiness and cutting force. Sensory analysis showed that fermented sausages manufactured with Pronase E and Penicillium aurantiogriseum extract had better odour, flavour, texture and, as a consequence, better general acceptability.
Ana L. F. Porto - One of the best experts on this subject based on the ideXlab platform.
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Antimicrobial and radical scavenging properties of bovine collagen hydrolysates produced by Penicillium aurantiogriseum URM 4622 collagenase
Journal of Food Science and Technology, 2015Co-Authors: Carolina A. Lima, Júlia Furtado Campos, José L. Lima Filho, Attilio Converti, Maria G. Carneiro Cunha, Ana L. F. PortoAbstract:A 2^3 full factorial design was used to identify the main effects and interactions of pH, collagen concentration and temperature on the degree of collagen hydrolysis (DH) by collagenase from Penicillium aurantiogriseum URM 4622. Increases in both pH and collagen concentration improved DH, and a positive interaction effect was observed for these variables. On the other hand, temperature had a negative main effect on DH. The maximum value of DH (4.65 μg/mL) was achieved at 7.5 mg/mL collagen concentration, pH 8.0 and 25 °C. The peptide profile showed several peptides with molecular weights lower than 2 kDa and exhibited antibacterial activity against Escherichia coli , Bacillus subtilis and Staphylococcus aureus . An antioxidant activity of 84.7 ± 0.24 % towards the radical ABTS• + was obtained with 50 mg/mL hydrolysates. This study demonstrated that collagen hydrolysed by P. aurantiogriseum URM 4622 collagenase possesses interesting antibacterial and antioxidant activities.
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Production and characterization of a collagenolytic serine proteinase by Penicillium aurantiogriseum URM 4622: A factorial study
Biotechnology and Bioprocess Engineering, 2011Co-Authors: Carolina A. Lima, Maria G. Carneiro-da-cunha, José L. Lima Filho, Attilio Converti, Benício B. Neto, Ana L. F. PortoAbstract:A 2^4 full factorial design was used to identify the main effects and interactions of the initial medium pH, soybean flour concentration, temperature and orbital agitation speed on extracellular collagenase production by Penicillium aurantiogriseum URM4622. The most significant variables for collagenase production were soybean flour concentration and initial medium pH that had positive main effects, and temperature that had a negative one. Protein concentration in soybean flour revealed to be a significant factor for the production of a collagenase serine proteinase. The most favorable production conditions were found to be 0.75% soybean flour, pH 8.0, 200 rpm, and 28°C, which led to a collagenase activity of 164 U. The enzyme showed an optimum activity at 37°C and pH 9.0, was stable over wide ranges of pH and temperature (6.0 ∼ 10.0 and 25 ∼ 45°C, respectively) and was strongly inhibited by 10 mM phenylmethylsulphonylfluoride. The firstorder rate constants for collagenase inactivation in the crude extract, calculated from semi-log plots of the residual activity versus time, were used in Arrhenius and Eyring plots to estimate the main thermodynamic parameters of thermoinactivation ( E *_ d = 107.4 kJ/mol and ΔH*_ d = 104.7 kJ/mol). The enzyme is probably an extracellular neutral serine collagenase effective on azocoll, gelatin and collagen decomposition.