Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Cunha, Aline G.; Fernández‐Lorente, Gloria; Gutarra, Melissa Limoeiro Estrada; Bevilaqua, Juliana V.; Almeida, Rodrigo Volcan; Paiva, Lucia Moreira Campos; Fernández‐Lafuente, Roberto; Guisán, José M.; Freire, Denise Maria Guimarães

doi:10.1007/s12010-008-8425-7

Cited by 26 publications

(17 citation statements)

References 27 publications

(36 reference statements)

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“…Cunha et al [83] studied the purification/immobilization of a “pool” of lipases from P. simplicissimum produced by SSF using babassu cake as a culture medium. The process undertaken by means of sequential immobilization in hydrophobic supports (butyl, phenyl, and octyl agarose) resulted in three fractions with distinct thermal stability, specificity, and enantioselectivity properties.…”

Section: Enzyme Production and Characteristicsmentioning

confidence: 99%

Production and Use of Lipases in Bioenergy: A Review from the Feedstocks to Biodiesel Production

et al. 2011

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Lipases represent one of the most reported groups of enzymes for the production of biofuels. They are used for the processing of glycerides and fatty acids for biodiesel (fatty acid alkyl esters) production. This paper presents the main topics of the enzyme-based production of biodiesel, from the feedstocks to the production of enzymes and their application in esterification and transesterification reactions. Growing technologies, such as the use of whole cells as catalysts, are addressed, and as concluding remarks, the advantages, concerns, and future prospects of enzymatic biodiesel are presented.

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Section: Enzyme Production and Characteristicsmentioning

confidence: 99%

Production and Use of Lipases in Bioenergy: A Review from the Feedstocks to Biodiesel Production

et al. 2011

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“…Enzyme immobilization ensures recycling of the biocatalyst, allows easy product separation, and may improve performance of the enzyme [4]. The kinetic behavior of free enzymes is different from the one shown by immobilized forms due to conformational changes, steric hindrance, substrate and products partition, and microenvironmental and diffusion effects.…”

Section: Introductionmentioning

confidence: 99%

Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase ofAspergillus nidulans

et al. 2013

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The recombinant NStcI A. nidulans esterase was adsorbed on Accurel MP1000, where protein yield and immobilization efficiency were 42.48% and 81.94%, respectively. Storage stability test at 4°C and RT showed 100% of residual activity after 40 days at both temperatures. The biocatalyst retains more than 70% of its initial activity after 3 cycles of repeated use. Biochemical properties of this new biocatalyst were obtained. Maximum activity was achieved at pH 11 and 30°C, while the best stability was observed with the pH between 9 and 11 at 40°C. NStcI thermostability was increased after immobilization, as it retained 47.5% of its initial activity after 1 h at 60°C, while the free enzyme under the same conditions displayed no activity. NStcI preserved 70% of its initial activity in 100% hexane after 72 h. Enzymatic kinetic resolution of (R,S)-1-phenylethanol was chosen as model reaction, using vinyl acetate as acyl donor. After optimization of reaction parameters, the highest possible conversion (42%) was reached at 37°C, a w of 0.07, and 120 h of bioconversion in hexane with an enantiomeric excess of 71.7%. NStcI has selectivity for (R)-enantiomer. The obtained E value (31.3) is in the range considered useful to resolve enantiomeric mixtures.

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“…The immobilization was conducted for 25 h at 17 °C under mild stirring (36 rpm). During enzyme immobilization, aliquots of 150 µL were withdrawn (0, 0.5, 1, 3, 6, 25 h) for determination of the hydrolytic activity of the enzyme still present in the supernatant, using p ‐NPL as substrate . Finally, the biocatalysts (immobilized enzymes) obtained at the end of the immobilization process were washed with distilled water, filtrated, dried in desiccators, and stored in the refrigerator (17 °C).…”

Section: Methodsmentioning

confidence: 99%

Effects of Reaction Operation Policies on Properties of Core–Shell Polymer Supports Used for Preparation of Highly Active Biocatalysts

Pinto

Castro

Cipolatti

et al. 2018

Macro Reaction Engineering

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Core–shell polymer supports with different morphological features and compositions are prepared through combined suspension and emulsion polymerizations. It is shown that proper manipulation of the divinylbenzene (DVB) feed content allows for maximization of specific areas, porosities, and mechanical resistances. Additionally, it is shown that feeding of previously prepared miniemulsions leads to core–shell particles with smaller specific areas, due to less efficient coating of the cores. Particularly, the combined manipulation of polymerization times and DVB feed compositions allows for production of particles with pronounced specific area (50 m2 g−1) and porosity (0.30 cm3 g−1). Produced core–shell polymer particles are employed as supports for the immobilization of lipase B from Candida antarctica, and the obtained enzymatic activities for both hydrolysis (A hyd) and esterification (A est) reactions are very high (A hyd = 34.7 ± 3.8 U/g; A est = 3564.6 ± 581 U/g), even when compared to activities obtained using the reference commercial biocatalyst Novozym 435 (A hyd = 7.6 ± 1.8 U/g, A est = 2384.7 ± 307.2 U/g). Finally, biocatalysts prepared with the core–shell supports present higher enzymatic activities than biocatalysts prepared with supports of higher specific area obtained through conventional emulsion polymerizations, indicating that the porous structure of the shell can be beneficial for the immobilization and activity of the enzymes.

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Separation and Immobilization of Lipase from Penicillium simplicissimum by Selective Adsorption on Hydrophobic Supports

Cited by 26 publications

References 27 publications

Production and Use of Lipases in Bioenergy: A Review from the Feedstocks to Biodiesel Production

Production and Use of Lipases in Bioenergy: A Review from the Feedstocks to Biodiesel Production

Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase ofAspergillus nidulans

Effects of Reaction Operation Policies on Properties of Core–Shell Polymer Supports Used for Preparation of Highly Active Biocatalysts

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