Recovery of pectinases from Aspergillus niger using aqueous two-phase systems / Recuperação de pectinases de Aspergillus niger usando sistemas aquosos bifásicos

This work aimed to study the purification of pectinases by aqueous two-phase systems (ATPS). The crude enzymatic extract was produced by Aspergillus niger ATCC 9642 and contained exo-polygalacturonase (exo-PG), pectinmethylesterase (PME) and pectin lyase (PMGL). The ATPS systems tested consisted in the combinations of polyethylene glycol (PEG) and potassium phosphate and sodium citrate, alcohol (ethanol, n-propanol and isopropanol) and salt (ammonium sulfate, potassium phosphate and sodium citrate). The experiments showed higher recoveries using ATPS system - PEG/phosphate for the exo-PG were using 16% PEG 4.0 kDa/4.8% NaCl and 16% PEG 1.5 kDa/without NaCl, obtaining purification factors (PF) of 1.37 and 1.21 times and recovery (R) of 49 and 59%, respectively. However, for the enzymes PME and PMGL were of 4.8 and 4.7 fold and 478 and 241%, respectively. When used ATPS system - PEG/sodium citrate the best PF were of 2.4, 7.85 and 5.7 and R of 100, 331 and 239% for exo-PG, PME and PMGL, respectively. The ATPS system is an alternative and efficient method for the recovery and/or purification of pectinases. This work aimed to study the purification of pectinases by aqueous two-phase systems (ATPS). The crude enzymatic extract was produced by Aspergillus niger ATCC 9642 and contained exo-polygalacturonase (exo-PG), pectinmethylesterase (PME) and pectin lyase (PMGL). The ATPS systems tested consisted in the combinations of polyethylene glycol (PEG) and potassium phosphate and sodium citrate, alcohol (ethanol, n-propanol and isopropanol) and salt (ammonium sulfate, potassium phosphate and sodium citrate). The experiments showed higher recoveries using ATPS system - PEG/phosphate for the exo-PG were using 16% PEG 4.0 kDa/4.8% NaCl and 16% PEG 1.5 kDa/without NaCl, obtaining purification factors (PF) of 1.37 and 1.21 times and recovery (R) of 49 and 59%, respectively. However, for the enzymes PME and PMGL were of 4.8 and 4.7 fold and 478 and 241%, respectively. When used ATPS system - PEG/sodium citrate the best PF were of 2.4, 7.85 and 5.7 and R of 100, 331 and 239% for exo-PG, PME and PMGL, respectively. The ATPS system is an alternative and efficient method for the recovery and/or purification of pectinases. This work aimed to study the purification of pectinases by aqueous two-phase systems (ATPS). The crude enzymatic extract was produced by Aspergillus niger ATCC 9642 and contained exo-polygalacturonase (exo-PG), pectinmethylesterase (PME) and pectin lyase (PMGL). The ATPS systems tested consisted in the combinations of polyethylene glycol (PEG) and potassium phosphate and sodium citrate, alcohol (ethanol, n-propanol and isopropanol) and salt (ammonium sulfate, potassium phosphate and sodium citrate). The experiments showed higher recoveries using ATPS system - PEG/phosphate for the exo-PG were using 16% PEG 4.0 kDa/4.8% NaCl and 16% PEG 1.5 kDa/without NaCl, obtaining purification factors (PF) of 1.37 and 1.21 times and recovery (R) of 49 and 59%, respectively. However, for the enzymes PME and PMGL were of 4.8 and 4.7 fold and 478 and 241%, respectively. When used ATPS system - PEG/sodium citrate the best PF were of 2.4, 7.85 and 5.7 and R of 100, 331 and 239% for exo-PG, PME and PMGL, respectively. The ATPS system is an alternative and efficient method for the recovery and/or purification of pectinases

Coastal marine data crowdsourcing using the Internet of Floating Things: Improving the results of a water quality model

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Processo para a esterificação de cargas vegetais

DepositadaA presente invenção descreve um processo para a esterificação de cargas vegetais, o qual compreende a reação de uma corrente de ácidos graxos livres com uma quantidade estequiométrica ou excesso de um álcool em um solvente gasoso pressurizado utilizando catálise enzimática

'Synthetic lipase' production from a newly isolated Sporidiobolus pararoseus strain by submerged fermentation

The lipase produced by a newly isolate Sporidiobolus pararoseus strain has potential catalysis ability for esterification reactions. In order to improve its synthetic activity, this work aimed at optimizing 'synthetic lipase' production by submerged fermentation of a conventional media based on peptone, yeast extract, NaCl and olive oil using experimental design technique. According to the results obtained in the first experimental design (2(4-1)), yeast extract and NaCl concentrations were tested to further optimization by response surface methodology. The maximum 'synthetic lipase' activity obtained was 26.9 U/mL in the optimized media (5.0, 6.8, 7.0 and 1.0% (wt/v) of peptone, yeast extract, NaCl and olive oil, respectively), representing a 6.36-fold increase compared to the initial medium. The time course of 'synthetic lipase' production in the optimized condition was evaluated in terms of synthetic activity, protease activity, biomass and total carbon and the maximum synthetic activity was observed during the stationary phase of growth

Concentration, characterization and application of lipases from Sporidiobolus pararoseus strain

Lipases produced by a newly isolated Sporidiobolus pararoseus strain have potential catalytic ability for esterification reactions. After production, the enzymatic extracts (conventional crude and precipitated, 'CC' and 'CP', and industrial crude and precipitated, 'IC' e 'IP') were partially characterized. The enzymes presented, in general, higher specificity for short chain alcohols and fatty acids. The precipitated extract showed a good thermal stability, higher than that for crude enzymatic extracts. The 'CC' and 'CP' enzymes presented high activities after exposure to pH 6.5 and 40 ºC. On the other hand, the 'IC' and 'IP' extracts kept their activities in a wide range of pH memory but presented preference for higher reaction temperatures. Preliminary studies of application of the crude lipase extract in the enzymatic production of geranyl propionate using geraniol and propionic acid as substrates in solvent-free system led to a reaction conversion of 42 ± 1.5%