Lígia Maria Gonçalves Fernandes, Jônatas de Carvalho-Silva, William Eugenio Lopes da Silva, Márcia Nieves Carneiro da Cunha, Attilio Converti, Tatiana Souza Porto
{"title":"在大豆农工业残渣中扩大异形曲霉 URM0269 胶原酶的优化生产规模。","authors":"Lígia Maria Gonçalves Fernandes, Jônatas de Carvalho-Silva, William Eugenio Lopes da Silva, Márcia Nieves Carneiro da Cunha, Attilio Converti, Tatiana Souza Porto","doi":"10.1016/j.ijbiomac.2024.137734","DOIUrl":null,"url":null,"abstract":"<p><p>Collagenase and protease productions from Aspergillus heteromorphus URM0269 were optimized by submerged fermentation using soybean flour as substrate. Fermentations were performed according to composite design using the concentrations of substrate and yeast extract as the independent variables. The best condition was scaled up in a stirred tank bioreactor to assess the fermentation kinetics. The highest production of both enzymes occurred at concentrations of 2.0 % substrate and 0.1 % yeast extract. Contrariwise, after scale-up, collagenase activity increased from 33.5 to 148.5 U/mL, while the protease decreased from 16.3 to 11.7 U/mL. A. heteromorphus URM0269 showed a maximum growth rate of 0.09 h<sup>-1</sup> and yields of protease and collagenase on biomass, after 65 h of 2.70 and 34.22 U/mgx, respectively. Collagenase acted optimally at 40 °C and pH 6.0 on collagen as a substrate and displayed an allosteric trend, achieving a maximum reaction rate of 132.47 U/mL. Thermodynamic parameters of collagen degradation such as Gibbs free energy (74.16 kJ/mol), enthalpy (11.64 kJ/mol), entropy (-199.63 J/K.mol), and activation energy (14.25 kJ/mol) were determined for optimal temperature. These results demonstrated that soybean flour is a potential agroindustrial residue for collagenase production. Furthermore, the collagenase displayed promising biochemical and thermodynamic features for other biotechnological applications.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"137734"},"PeriodicalIF":7.7000,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Scaling up the optimized production of Aspergillus heteromorphus URM0269 collagenase in soybean agroindustrial residue.\",\"authors\":\"Lígia Maria Gonçalves Fernandes, Jônatas de Carvalho-Silva, William Eugenio Lopes da Silva, Márcia Nieves Carneiro da Cunha, Attilio Converti, Tatiana Souza Porto\",\"doi\":\"10.1016/j.ijbiomac.2024.137734\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Collagenase and protease productions from Aspergillus heteromorphus URM0269 were optimized by submerged fermentation using soybean flour as substrate. Fermentations were performed according to composite design using the concentrations of substrate and yeast extract as the independent variables. The best condition was scaled up in a stirred tank bioreactor to assess the fermentation kinetics. The highest production of both enzymes occurred at concentrations of 2.0 % substrate and 0.1 % yeast extract. Contrariwise, after scale-up, collagenase activity increased from 33.5 to 148.5 U/mL, while the protease decreased from 16.3 to 11.7 U/mL. A. heteromorphus URM0269 showed a maximum growth rate of 0.09 h<sup>-1</sup> and yields of protease and collagenase on biomass, after 65 h of 2.70 and 34.22 U/mgx, respectively. Collagenase acted optimally at 40 °C and pH 6.0 on collagen as a substrate and displayed an allosteric trend, achieving a maximum reaction rate of 132.47 U/mL. Thermodynamic parameters of collagen degradation such as Gibbs free energy (74.16 kJ/mol), enthalpy (11.64 kJ/mol), entropy (-199.63 J/K.mol), and activation energy (14.25 kJ/mol) were determined for optimal temperature. These results demonstrated that soybean flour is a potential agroindustrial residue for collagenase production. 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Scaling up the optimized production of Aspergillus heteromorphus URM0269 collagenase in soybean agroindustrial residue.
Collagenase and protease productions from Aspergillus heteromorphus URM0269 were optimized by submerged fermentation using soybean flour as substrate. Fermentations were performed according to composite design using the concentrations of substrate and yeast extract as the independent variables. The best condition was scaled up in a stirred tank bioreactor to assess the fermentation kinetics. The highest production of both enzymes occurred at concentrations of 2.0 % substrate and 0.1 % yeast extract. Contrariwise, after scale-up, collagenase activity increased from 33.5 to 148.5 U/mL, while the protease decreased from 16.3 to 11.7 U/mL. A. heteromorphus URM0269 showed a maximum growth rate of 0.09 h-1 and yields of protease and collagenase on biomass, after 65 h of 2.70 and 34.22 U/mgx, respectively. Collagenase acted optimally at 40 °C and pH 6.0 on collagen as a substrate and displayed an allosteric trend, achieving a maximum reaction rate of 132.47 U/mL. Thermodynamic parameters of collagen degradation such as Gibbs free energy (74.16 kJ/mol), enthalpy (11.64 kJ/mol), entropy (-199.63 J/K.mol), and activation energy (14.25 kJ/mol) were determined for optimal temperature. These results demonstrated that soybean flour is a potential agroindustrial residue for collagenase production. Furthermore, the collagenase displayed promising biochemical and thermodynamic features for other biotechnological applications.
期刊介绍:
The International Journal of Biological Macromolecules is a well-established international journal dedicated to research on the chemical and biological aspects of natural macromolecules. Focusing on proteins, macromolecular carbohydrates, glycoproteins, proteoglycans, lignins, biological poly-acids, and nucleic acids, the journal presents the latest findings in molecular structure, properties, biological activities, interactions, modifications, and functional properties. Papers must offer new and novel insights, encompassing related model systems, structural conformational studies, theoretical developments, and analytical techniques. Each paper is required to primarily focus on at least one named biological macromolecule, reflected in the title, abstract, and text.