50 research outputs found
Isomaltulose: The Next Sweetener, A Quick Review
No full textThe social behavior of new generations consume highly processed foods and high levels of fat and sugar, such as glucose or high-fructose syrup (corn syrup), commonly used in the manufacture of hard candies, have generated a growing increase in cases of diabetes and nutrition problems. In this context, we present the isomaltulose as a substitute potential for sweeteners, due to its property of maintaining stable glycemic levels, dosing energy to the organism in a long-term way, promoting the fat oxidation and it is a noncariogenic food. There is just one company that distributes isomaltulose in an industry level, under the name of Palatinose™ (Beneo-Palatinti, Sudzücker Group, Mannheim, Germany) and already incorporated isomaltulose products in the food processing as beverage, bakery, energy drinks, dry-powder drinks, chewing gum, hard candies, and others. But it is necessary to produce quantities of isomaltulose that will supply the demand of the food industry. The latest advances in biotechnology provide tools to efficiently produce 278any product that may result from the metabolism of micro-organisms. But first, it is important to know the global aspects of the enzyme, the reaction that catalyzes and its products to determine their chemical and biological parameters. This work aims to make a quick review of all these aspects that allow us to understand and start the biotechnological path for the design and development of future foods based on isomaltulose.Fil: Bracho Oliveros, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Ramírez Gutiérrez, Andrea Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Ortiz, Gastón Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Contreras Esquivel, Juan Carlos. Universidad Autónoma de Coahuila; MéxicoFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentin
Kinetic modelling of thermal inactivation of a keratinase from Purpureocillium lilacinum LPSC # 876 and the influence of some additives on its thermal stability
No full textThermal inactivation of a keratinase produced by Purpureocillium lilacinum LPSC #876 was kinetically investigated using several enzyme inactivation models at the temperature range of 50–65 °C. Among the models studied, the Weibull distribution was the best model that describes the residual activity of P. lilacinum keratinase after heat treatment over the selected temperatures. The stabilising effect of metal ions (Ca2+ or Mg2+, 5 mmol l−1 ) or polyols (propylene glycol and glycerol, 10 % v/v) was investigated, showing that the presence of Ca2+ increases the enzyme stability significantly. Conforming to the increased Ca2+ concentration, thermal stability of the enzyme also increased, with 10 mM of Ca2+ being the concentration of metal in which the enzyme retained 100 % of its original activity after being incubated for 1 h at 55 °C. The effects of temperature on Weibull equation parameters and on the characteristics of the inactivation curves were evaluated. In the absence of any additives (control), the reliable time (tR) of the keratinase, analogous to D value, ranged from 484.16 to 63.67 min, while in the presence of Ca2+ the tR values ranged from 6,221 to 414.95 min at 50– 65 °C. P. lilacinum keratinase is a potentially useful biocatalyst, and therefore, kinetic modelling of thermal inactivation addresses an important topic for its application in various industrial processes.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentin
Protopectinasa-se de Geotrichum klebahnii: Estudios de adsorción y capacidad de solubilización de pectina
No full textProtopectinasa-SE (PPasa-SE) es una poligalacturonasa producida por Geotrichum klebahnii con capacidad de liberar pectina por hidrólisis de protopectina. La reacción de liberación de pectina responde a un sistema de catálisis heterogenea, donde la interacción enzima-protopectina y la liberación de pectina, son objetivos de esta investigación. La interacción enzima-protopectina resultó dependiente del tamaño y estructura de las partículas del sustrato, así como de la naturaleza de la solución amortiguadora. Para partículas pequeñas la cinética de adsorción siguió un comportamiento definido por la isoterma de Langmuir. La reacción respondió al modelo cinético de Michaelis-Menten, con valores de Km y Vmax de 30.2 g/L y 57.3 g/L.h. Los mejores resultados en cuanto a la adsorción de la enzima y la solubilización de pectina fueron obtenidos con una solución amortiguadora de citrato y citrato-fosfato. Este trabajo constituye un primer reporte en cuanto a la solubilización de pectina que involucra un modelo de unión al sustrato asociado en sistemas pectinasa-protopectinasa.Protopectinase SE (PPase-SE) is a polygalacturonase produced by Geotrichum klebahnii with the capacity to liberate pectin through protopectin hydrolysis. The protopectin cleavage is a typical heterogeneous-catalysis reaction whose interaction between the enzyme and the protopectin substrate from lemon albedo along with the release of the pectin-reaction product were the objectives of this investigation. The interaction between PPase-SE and protopectin depended on the particle size and the structure of the substrate as well as on the nature of the buffer. The adsorption kinetics follows, for small particles, a Langmuir isotherm pattern. The reaction exhibited Michaelis-Menten kinetics, giving respective apparent-Km and Vmax values of 30.2 g/l and 57.3 g/l.h. The better results in enzyme adsorption and pectin releasing were obtained with citrate and citrate-phosphate buffers. This report constitutes the first investigation in pectin solubilization involving a model for the substrate-binding mechanism within the pectinase-protopectinase system.Fil: Zapata Zapata, Arley David. Universidad Nacional de Colombia; ColombiaFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentin
Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
No full textKeratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50 °C after 1 h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; ArgentinaFil: Contreras Esquivel, Juan Carlos. Universidad Autónoma de Coahuila; MéxicoFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentin
Enzymatic hydrolysis of gelatin layers of X-ray films and release of silver particles using keratinolytic serine proteases from Purpureocillium lilacinum LPS # 876
No full textEnzymatic decomposition of gelatin layers on used X-ray films and repeated utilization of the enzyme for potential application in silver recovery were investigated using keratinolytic serine proteases from Purpureocillium lilacinum LPS # 876. At pH 9.0, the enzymatic reaction was enhanced by the increase of enzyme concentration or by the increase of the temperature up to 60oC. Under the conditions of 6.9 U/ml, 60oC, and pH 9.0, hydrolysis of the gelatin layers and the resulting release of silver particles were achieved within 6 min. The protective effect of polyols against thermal denaturation was investigated. The presence of glycerol and propylene glycol increased enzyme stability. When the reusability of the enzyme for gelatin hydrolysis was tested, it could be seen that it could be effectively reused for more cycles when glycerol was added, compared with the enzyme without protective agents. The results of these repeated treatments suggested that a continuous process of recycling silver from used X-ray is feasible. Keeping in mind that recycling is (at the present time) needed and imperative, it can be remarked that, in this research, three wastes were successfully used: hair waste in order to produce serine proteases; glycerol in order to enhance enzyme thermal stability; and used Xray films in order to recover silver and PET films.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentin
Control of agitation rate and aeration for enhanced polygalacturonase production in submerged fermentation by Aspergillus sojae using agro-industrial wastes
No full textBACKGROUND: The koji mold Aspergillus sojae, an industrially important microorganism, can produce high levels of pectinases utilizing agro-industrial wastes. This study introduces apricot and peach pomace, two agro-industrial wastes barely considered as raw material for the generation of value-added products, and focuses on its utilization together with orange peel for polygalacturonase production in submerged cultures using A. sojae. RESULTS: A Doehlert response surface methodology design conducted in shake flasks and applied individually with these three by-products led to 60–80 U mL−1 polygalacturonase activity. In bioreactor studies performed with a mixture of apricot pomace and orange peel, by fixing stirrer speed to 600 rpm and cascading airflow to the dissolved oxygen tension up to 1.7 vvm, oxygen limitation problems were overcome and polygalacturonase activity values of 380 U mL−1 were achieved. CONCLUSION: A simple and efficient strategy to minimize oxygen limitation with the lowest possible shear stress is provided for stirred-tank bioreactors working with highly viscous broths, so as to ultimately enhance microbial enzyme production. The polygalacturonase activity yields obtained in our study are among the highest reported in the literature.Fil: Fratebianchi de la Parra, Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Crespo, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Tari, Canan. Izmir Institute of Technology; TurquíaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentin
Evaluation of agro-industrial wastes, their state and mixing ratio for maximum polygalacturonase and biomass production in submerged fermentation
No full textThe potential of important agro-industrial wastes, apple pomace (AP) and orange peel (OP) as C sources, was investigated in the maximization of polygalacturonase (PG), an industrially significant enzyme, using an industrially important microorganism Aspergillus sojae. Factors such as various hydrolysis forms of the C sources (hydrolysed-AP, non-hydrolysed-AP, hydrolysed-AP + OP, non-hydrolysed-AP + OP) and N sources (ammonium sulphate and urea), and incubation time (4, 6, and 8 days) were screened. It was observed that maximum PG activity was achieved at a combination of non-hydrolysed-AP + OP and ammonium sulphate with eight days of incubation. For the pre-optimization study, ammonium sulphate concentration and the mixing ratios of AP + OP at different total C concentrations (9, 15, 21 g l−1) were evaluated. The optimum conditions for the maximum PG production (144.96 U ml−1) was found as 21 g l−1 total carbohydrate concentration totally coming from OP at 15 g l−1 ammonium sulphate concentration. On the other hand, 3:1 mixing ratio of OP + AP at 11.50 g l−1 ammonium sulphate concentration also resulted in a considerable PG activity (115.73 U ml−1). These results demonstrated that AP can be evaluated as an additional C source to OP for PG production, which in turn both can be alternative solutions for the elimination of the waste accumulation in the food industry with economical returns.Fil: Göğüş, Nihan. Izmir Institute of Technology; TurquíaFil: Evcan, Ezgi. Izmir Institute of Technology; TurquíaFil: Tari, Canan. Izmir Institute of Technology; TurquíaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentin
Bioprocessing of “Hair Waste” by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
No full textPaecilomyces lilacinus (Thom) Samson LPS 876, a locally isolated fungal strain, was grown on minimal mineral medium containing “hair waste,” a residue from the hair-saving unhairing process, and produced a protease with keratinolytic activity. This enzyme was biochemically characterized. The optimum reaction conditions, determined with a response surface methodology, were 60°C and pH 6.0. It was remarkably stable in a wide range of pHs and temperatures. Addition of Ca2+, Mg2+, or sorbitol was found to be effective in increasing thermal stability of the protease. PMSF and Hg2+ inhibited the proteolytic activity indicating the presence of a thiol-dependent serine protease. It showed high stability toward surfactants, bleaching agents, and solvents. It was also compatible with commercial detergents (7 mg/mL) such as Ariel, Skip, Drive, and Ace, retaining more than 70% of its proteolytic activity in all detergents after 1 h of incubation at 40°C. Wash performance analysis revealed that this protease could effectively remove blood stains. From these properties, this enzyme may be considered as a potential candidate for future use in biotechnological processes, as well as in the formulation of laundry detergents.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentin
Aportes para la degradación biológica de residuos sólidos de curtiembre
No full textEl proceso de depilado conservador del pelo tiene como beneficio hacia el medio ambiente una disminución de la contaminación en el efluente líquido de ribera, pero como contraparte, durante este procedimiento se genera un nuevo residuo sólido llamado "residuo pelo" que debe ser apropiadamente dispuesto.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Galarza, Betina Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Instituto Nacional de Tecnología Industrial. Centro de Investigación y Desarrollo del Cuero; ArgentinaFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Cantera, Carlos. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Instituto Nacional de Tecnología Industrial. Centro de Investigación y Desarrollo del Cuero; Argentin
Purification and Biochemical and Kinetic Properties of an Endo-Polygalacturonase from the Industrial Fungus Aspergillus sojae
No full textAn endo-polygalacturonase secreted by Aspergillus sojae was characterized after being purified to homogeneity from submerged cultures with orange peel as the sole carbon source by gel filtration and ion-exchange chromatographies. According to SDS-PAGE and analytical isoelectric focusing analyses, the enzyme presents a molecular weight of 47 kDa and pI value of 4.2. This enzyme exhibits considerable stability under highly acidic to neutral conditions (pH 1.5-6.5) and presents a half-life of 2 h at 50°C. Besides its activity towards pectin and polygalacturonic acid, the enzyme displays pectin-releasing activity, acting best in a pH range of 3.3-5.0. Thin-layer chromatographic analysis revealed that tri-galacturonate is the main enzymatic end product of polygalacturonic acid hydrolysis, indicating that it is an endo-polygalacturonase. The enzyme exhibits Michaelis-Menten kinetics, with KM and VMAX values of 0.134 mg/mL and 9.6 μmol/mg/min, respectively, and remained stable and active in the presence of SO2, ethanol, and various cations assayed except Hg2+.Fil: Fratebianchi de la Parra, Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentin
