Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Illanes, Andrés; González, José M.; Gómez, José Manuel; Valencia, Pedro; Wilson, Lorena

doi:10.2225/vol13-issue1-fulltext-12

Cited by 20 publications

(14 citation statements)

References 35 publications

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“…These results can be explained by steric effects of large PHB beads (LPHB) which had significant influence on the lipase conformation, leading to the changes of the enzyme activity or diffusional limitations that restricted the contact between the active site of the lipase and substrate (olive oil). It is well known that diffusional limitations become more a restraining factor as the diameter of the support beads increases [13,26,27,69]. Results displayed in Table 2 show that the specific activity of the biocatalysts, ratio between hydrolytic activity and immobilized protein amount, also decreased after immobilization on LPHB.…”

Section: Immobilization Of Lipases On Sphb and Lphb Beadsmentioning

confidence: 93%

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Mendes

Oliveira

Velez

et al. 2012

International Journal of Biological Macromolecules

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Five microbial lipase preparations from several sources were immobilized by hydrophobic adsorption on small or large poly-hydroxybutyrate (PHB) beads and the effect of the support particle size on the biocatalyst activity was assessed in the hydrolysis of olive oil, esterification of butyric acid with butanol and transesterification of babassu oil (Orbignya sp.) with ethanol. The catalytic activity of the immobilized lipases in both olive oil hydrolysis and biodiesel synthesis was influenced by the particle size of PHB and lipase source. In the esterification reaction such influence was not observed. Geobacillus thermocatenulatus lipase (BTL2) was considered to be inadequate to catalyze biodiesel synthesis, but displayed high esterification activity. Butyl butyrate synthesis catalyzed by BTL2 immobilized on small PHB beads gave the highest yield (≈90 mmol L(-1)). In biodiesel synthesis, the catalytic activity of the immobilized lipases was significantly increased in comparison to the free lipases. Full conversion of babassu oil into ethyl esters was achieved at 72 h in the presence of Pseudozyma antarctica type B (CALB), Thermomyces lanuginosus lipase (Lipex(®) 100 L) immobilized on either small or large PHB beads and Pseudomonas fluorescens (PFL) immobilized on large PHB beads. The latter preparation presented the highest productivity (40.9 mg of ethyl esters mg(-1) immobilized protein h(-1)).

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Section: Immobilization Of Lipases On Sphb and Lphb Beadsmentioning

confidence: 93%

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Mendes

Oliveira

Velez

et al. 2012

International Journal of Biological Macromolecules

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“…The relatively low apparent enzymatic activity with respect to the amounts of protein effectively loaded, 9 U instead of 33 U (Fig. 3a), i.e., *30 %, is therefore likely due mostly to enzymes located at the surface of the particles [35].…”

Section: Immobilized Enzymatic Activitymentioning

confidence: 97%

“…In particular, it is likely that, in the case of MCM-41, because the protein is too large to enter the porosity, most of the protein is adsorbed on the outer surface of the particles with direct access to the substrate at the bulk concentration. The diffusion constraints are those that apply to catalytic species attached to a flat surface [35]. Another smaller proportion of the enzyme can be positioned at the mouth of the pores with less accessibility to the substrate.…”

Section: Immobilized Enzymatic Activitymentioning

confidence: 99%

Protected activity of a phytase immobilized in mesoporous silica with benefits to plant phosphorus nutrition

Trouillefou

Cadre

Cacciaguerra

et al. 2014

J Sol-Gel Sci Technol

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Phosphorus (P) is one of the main nutrients required for plant growth and is absorbed and metabolized in the form of orthophosphate ions (Pi). In agriculture, P is a major component of fertilizers. Forecast shortages in P mine stocks within the coming decades call for alternative sources of this element for agricultural use. In the present study, we explore the possibility of incorporating phytase near the plant root system. Phytase is an enzyme capable of mobilizing the main organic form of P as phytate, which can represent up to 90 % of the total P stock in soils. We report the immobilization of phytase in KIT-6 silica mesoporous materials with large pores of 8.6 nm. The enzymatic activity is localized in the porous network, and the main kinetic features of the free phytase appear to be maintained within the functional material (pHopt = 5–5.5 and T opt = 55 °C). Most importantly, the enzyme immobilized in the pores shows a higher temperature stability and appears to be protected from protease degradation. Finally, phytase-loaded KIT-6 proved efficient at hydrolyzing phytate and delivering inorganic P to growing Medicago truncatula plants, which accumulated this newly available P in both roots and shoot

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“…[14][15][16][17][18][19][20][21][22][23][24][25] However, increased catalytic activity is generally limited due to mass transfer limitations between the enzyme and the substrate and conformational changes in the enzyme. [26][27][28][29][30][31][32][33][34] Therefore, there is still a high demand for immobilized enzymes with enhanced catalytic activity and stability.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of copper ion incorporated horseradish peroxidase-based hybrid nanoflowers for enhanced catalytic activity and stability

et al. 2015

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In this study, we report the preparation, catalytic activity and stability of a hybrid nanoflower (hNF) formed from horseradish peroxidase (HRP) enzyme and copper ions (Cu(2+)). We studied the morphology of hNFs as a function of the concentrations of copper (Cu(2+)) ions, chloride ions (Cl(-)) and HRP enzyme, the pH of the buffer solution (phosphate buffered saline), and the temperature of the reaction. The effects of morphology on the catalytic activity and stability of hNFs were evaluated by oxidation of guaiacol (2-methoxyphenol) to colored 3,3-dimethoxy-4,4-diphenoquinone in the presence of hydrogen peroxide (H2O2). The enhanced activity of hNFs synthesized (from 0.02 mg mL(-1) HRP in 10 mM PBS (pH 7.4) at +4 °C) was 17 595 U mg(-1), which was ∼300% higher than free HRP in PBS, where it achieved an activity of 5952 U mg(-1). In terms of stability, these hNFs stored in PBS buffer at +4 °C and room temperature (RT = 20 °C) lost 4% and 20%, respectively, of their initial catalytic activities within 30 days. Finally, we demonstrated that these hNFs can be utilized as sensors for the detection of dopamine.

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Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Cited by 20 publications

References 35 publications

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis

Protected activity of a phytase immobilized in mesoporous silica with benefits to plant phosphorus nutrition

Synthesis of copper ion incorporated horseradish peroxidase-based hybrid nanoflowers for enhanced catalytic activity and stability

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