Imobilização de lipases em filme de caseinato de sódio/glicerol: aplicação na síntese de ésteres

Sebrão, Damianni; Silva, Vanessa Dutra; Nascimento, Maria da Graça; Moreira, Matheus T.

doi:10.1590/s0100-40422007000500025

Cited by 9 publications

(8 citation statements)

References 32 publications

(60 reference statements)

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“…The conversions to pentyl oleate were obtained by nuclear magnetic resonance of hydrogen ( 1 H NMR) (Varian Unity Inova AC 500 MHz) through the comparison of the integrals of the hydrogen singlets of the alcohol and the hydrogen atoms of the ester. 34 On analyzing the 1 H NMR spectra for the alcohol and the ester a difference can be noted between the frequencies of the hydrogen peaks of the methylene group (-CH 2 ) bound to the oxygen atom, present in both molecules (RCH 2 OH; R'COOCH 2 R). The hydrogen atoms of the methylene group of the alcohol gave peaks at a lower frequency (more shielded) than those of the ester (less shielded) in the 1 H NMR spectra.…”

Section: Analytical Methodologymentioning

confidence: 99%

Potential application in biocatalysis of mycelium-bound lipases from Amazonian fungi

Zanotto¹,

Romano

Duvoisin

et al. 2009

J. Braz. Chem. Soc.

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Neste trabalho foram avaliados 212 fungos isolados de plantas da Região Amazônica quanto ao potencial de aplicação em biocatálise como fornecedores de lipases ligadas ao micélio. Estes isolados foram submetidos a ensaios de atividade hidrolítica e sintética. Quando submetidos ao ensaio com o substrato tributirina, 87% dos isolados apresentaram atividade hidrolítica. Destes, 30% mostraram bom crescimento em meio líquido indutor de lipase, e foram submetidos à avaliação sintética em reações de esterificação e transesterificação em solvente orgânico. Os nove fungos que apresentaram os melhores desempenhos sintéticos foram avaliados quanto a sua enantiosseletividade na reação de resolução do (R,S)-2-octanol. O isolado UEA_115 foi o biocatalisador mais versátil, apresentando bom desempenho nas reações de esterificação (conversão > 90%) e boa capacidade para a resolução do (R,S)-2-octanol (ee s 29%; ee p 99%; c 22%; E > 200). Com este estudo foi possível demonstrar o grande potencial dos fungos amazônicos como fornecedores de lipases para biocatálise.In this study, 212 fungi were isolated from Amazon region plants, aiming to obtain mycelium bound-lipase-producing biocatalysts. These isolates were submitted to hydrolytic and synthetic activity assays. When submitted to the tributyrine substrate test, 87% of the isolates showed hydrolytic activity. Of these, 30% showed good growth in lipase inducing liquid media and were submitted to evaluation of synthetic activity in esterification and transesterification reactions in organic solvents. The nine fungi which had the best synthetic activity were evaluated in the (R,S)-2-octanol resolution reaction, in order to verify the enantioselectivity of mycelium-bound lipases. The isolate UEA_115 was the most versatile biocatalyst, showing good performance in esterification reactions (conversion > 90%) and good ability for the resolution of (R,S)-2-octanol (ee s 29%; ee p 99%; c 22%; E > 200). Thus, this study has demonstrated the great potential of the Amazonian fungi as lipase suppliers for biocatalysts. Keywords: fungi, Amazon region, mycelium-bound lipase, biocatalyst screening, biocatalysis IntroductionIn recent years, global concern regarding the impact of human actions on the environment has been growing. The implementation of the concept of sustainable development in several productive activities has become an urgent issue. Fortunately, biotechnology also offers an increasing potential to meet the global demands for processes and products in greater harmony with the sustainability concept. 1,2 In this regard, one of the most promising tools in biotechnology is the field of applied biocatalysis, also referred to by some authors as biotransformation or enzymatic technology. 2,3 The advantages of using enzymes as biocatalysts in industrial processes have been shown to be ever more evident. Great versatility of catalyzed reactions, mild reaction conditions, and regio, chemo and enantioselective natures are those most frequently mentioned in the literature. 4 Such characteristic...

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Section: Analytical Methodologymentioning

confidence: 99%

Potential application in biocatalysis of mycelium-bound lipases from Amazonian fungi

Zanotto¹,

Romano

Duvoisin

et al. 2009

J. Braz. Chem. Soc.

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“…Where: Abs is the absorbance measured in the spectrophotometer; m is the slope for the DNS' method calibration curve (13,348 μmol Abs * mL ); F D is the dilution factor; t (10 min) is the incubation time; and V (mL) is the volume of sample containing the enzyme.…”

Section: Enzymatic Activity Assaymentioning

confidence: 99%

“…Such technique improves the properties of the biocatalyst by increasing the stability and rigidity of the structure, causing hyperhydrophilic microenvironments, which may protect the biocatalyst, and consequently reduce the inhibitions caused by irreversible / reversible inhibitors. However, one of the essential factors that must be considered when using a specific immobilization system is the type of interaction between the support and the biocatalyst, which can directly influence its stability and on the kinetic effects of catalysis [13].…”

mentioning

confidence: 99%

Immobilization of amylase using chitosan beads as support

et al. 2017

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Amylases are hydrolases that are prominent, compared to other enzymes, accounting for 65% of the world's market. They can be applied to any processes that require partial or complete hydrolysis of starch, such as: glucose production, the paper industry, brewing industry, food industry, among others. The use of enzymes in the industry brings great advantages, such as: a lower energy consumption; selectivity for the substrate; high activity and, in most cases, low production cost. However, it is still a costly catalytic route option, and it is necessary to use immobilization processes so that no further costs are generated in its recovery after the reaction. This work aimed to produce chitosan beads for use in the immobilization of amylase from a nonpurified source. The enzymatic broth volume evaluated was 7 and 10 mL, with the highest rate of immobilization (36.04%) and recovered activity (12.36%) achieved using 7 mL of enzymatic broth. In the evaluation of the number of spheres used for immobilization, 6, 10 and 14 units were evaluated. It was found that the smallest number of spheres was sufficient to immobilize 54.71% of the enzymes. However, the recovery activity was the lowest (6.77%). Immobilization by covalent bonding presented better immobilization result compared to other immobilizations (54.71%), despite the lower result for recovery of activity (6.77%).

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“…The enzyme stabilization is a desirable process from an economical point of view [4][5][6] . The immobilization of biocatalysts in innert supports (without damage to the enzyme activity) can ensure their use for several batches, resulting in economy for industrial processes 7 .…”

Section: Introductionmentioning

confidence: 99%

Screening of supports for immobilization of commercial porcine pancreatic lipase

et al. 2011

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The aim of this work is to report the performance of different supports for the immobilization of commercial porcine pancreatic lipase. The immobilization tests were carried out in several types of Accurel, activated alumina, kaolin, montmorillonite, ion exchange resins and zeolites. The characterization of the supports showed differences in terms of specific area and morphology. The characteristics of the supports influenced the amount of enzyme adsorbed, yield of immobilization and esterification activity of the resulting immobilized catalyst. The clays KSF and natural and pillared montmorillonites presented potential for use as support for lipase immobilization in terms of yield and esterification activity. Yields of immobilization of 76.32 and 52.01% were achieved for clays KSF and natural montmorillonite, respectively. Esterification activities of 754.03, 595.51, 591.88 and 515.71 U.g -1 were obtained for lipases immobilized in Accurel MP-100, Amberlite XAD-2, mordenite and pillared montmorillonite, respectively.

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Imobilização de lipases em filme de caseinato de sódio/glicerol: aplicação na síntese de ésteres

Cited by 9 publications

References 32 publications

Potential application in biocatalysis of mycelium-bound lipases from Amazonian fungi

Potential application in biocatalysis of mycelium-bound lipases from Amazonian fungi

Immobilization of amylase using chitosan beads as support

Screening of supports for immobilization of commercial porcine pancreatic lipase

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