Phytase Immobilization on Hydroxyapatite Nanoparticles Improves Its Properties for Use in Animal Feed

Coutinho, Thamara Carvalho; Tardioli, Paulo Waldir; Farinas, Cristiane S.

doi:10.1007/s12010-019-03116-9

Cited by 33 publications

(36 citation statements)

References 55 publications

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“…Enzyme–support adsorptions were performed in 2 mL tubes, using a support concentration of 0.05 g mL –1 in 20 mM acetate buffer (pH 5), with an enzymatic loading of 5 mg protein g –1 support, under gentle rotary stirring for 1 h, at 25 °C. The selected immobilization conditions and procedures were the same as those used previously for immobilization of the same enzymes on pure HA. − , The results were expressed in terms of the immobilization parameters: immobilization yield (IY), recovery activity (RA), and enzymatic activity of the final derivative ( A DE ), as described in the Supporting Information.…”

Section: Methodsmentioning

confidence: 99%

“…For β-glucosidase, it was possible to recycle the derivative and retain 70% of the initial activity during at least 10 hydrolysis cycles . For phytase, the derivative showed a broader profile of activity according to pH and temperature, with higher stability than the free enzyme at high temperatures, demonstrating its potential application in animal feed . For xylanase, the enzyme showed a higher affinity for the HA support modified with copper, demonstrating promising industrial applications .…”

Section: Introductionmentioning

confidence: 99%

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Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Coutinho

Malafatti

Paris

et al. 2020

ACS Appl. Nano Mater.

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Hydroxyapatite (HA) is an inorganic material with high ability to interact with proteins and has been recently explored as a support for enzyme immobilization. However, there are still some drawbacks concerning the recovery of these biocatalysts, which could be overcome using magnetic supports. Cobalt ferrite (CoFe 2 O 4 ) is a purely magnetic material, which offers excellent chemical stability, ease of synthesis, and mechanical hardness, being a promising candidate to form composites with HA and produce magnetic HA nanoparticles. Therefore, investigation of synthesis procedures and applications of HA/CoFe 2 O 4 composites to facilitate enzyme recovery by means of a magnetic field could find interest in a broad spectrum of biotechnological processes. Here, the co-precipitation method was used to synthesize HA/CoFe 2 O 4 composites with different HA/CoFe 2 O 4 mass ratios, for application as supports for enzyme immobilization. The enzymes β-glucosidase, phytase, and xylanase were selected for proof of concept due to their wide range of industrial applications. The composite with the highest cobalt ferrite content (2:1 mass ratio) was highly effective for immobilization of the three different enzymes, with immobilization yields (IYs) of 70−100% and recovered activities of 78−100%. The biocatalysts could be easily recovered from the reaction media by both centrifugation and application of an external magnetic field, demonstrating their potential for use in industrial processes. The materials exhibited good reusability, especially in the case of the βglucosidase biocatalyst, which could be reused 10 times, maintaining around 70% of its initial activity.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Coutinho

Malafatti

Paris

et al. 2020

ACS Appl. Nano Mater.

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“…These results indicated that Zeozyme NPs is highly resistant to trypsin and pepsin degradation, while the free xylanase is highly sensitive to pepsin and moderately resistant to trypsin. Enzyme immobilization moderately protected enzyme from denaturation in the acidic pH and proteases in gastrointestinal conditions such as phytase immobilized on hydroxyapatite NPs 41 . Thus, zeolite may play a suitable role in the stabilizing the xylanase against pepsin.…”

Section: Resultsmentioning

confidence: 99%

Zeolite-based nanocomposite as a smart pH-sensitive nanovehicle for release of xylanase as poultry feed supplement

Dashtestani

Ma’mani

Jokar

et al. 2021

Sci Rep

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Xylanase improves poultry nutrition by degrading xylan in the cell walls of feed grains and release the entrapped nutrients. However, the application of xylanase as a feed supplement is restricted to its low stability in the environment and gastrointestinal (GI) tract of poultry. To overcome these obstacles, Zeozyme NPs as a smart pH-responsive nanosystem was designed based on xylanase immobilization on zeolitic nanoporous as the major cornerstone that was modified with L-lysine. The immobilized xylanase was followed by encapsulating with a cross-linked CMC-based polymer. Zeozyme NPs was structurally characterized using TEM, SEM, AFM, DLS, TGA and nitrogen adsorption/desorption isotherms at liquid nitrogen temperature. The stability of Zeozyme NPs was evaluated at different temperatures, pH, and in the presence of proteases. Additionally, the release pattern of xylanase was investigated at a digestion model mimicking the GI tract. Xylanase was released selectively at the duodenum and ileum (pH 6–7.1) and remarkably preserved at pH ≤ 6 including proventriculus, gizzard, and crop (pH 1.6–5). The results confirmed that the zeolite equipped with the CMC matrix could enhance the xylanase thermal and pH stability and preserve its activity in the presence of proteases. Moreover, Zeozyme NPs exhibited a smart pH-dependent release of xylanase in an in vitro simulated GI tract.

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“…It has been purified from some plant sources and characterized (Gibson & Ullah, 1988;Konietzny et al, 1995;Mahajan & Dua, 1997;Phillippy, 1998;Greiner et al, 1998Greiner et al, , 2001Greiner & Alminger 1999;Greiner, 2002;Andriotis & Ross, 2003;Belho et al, 2016;Belho & Ambasht, 2017). Immobilization of phytase has been pursued mostly from microbial sources like Aspergillus ficuum (Liu et al, 1999;Moraes et al, 2008), A. niger (Menezes-Blackburn et al, 2011;Trouillefou et al, 2015;Coutinho et al, 2020), A. heteromorphus (Lata et al, 2014), Escherichia coli (Menezes-Blackburn et al, 2011;Cho et al, 2011;El-Shora et al, 2019), Candida krusei (Quan et al 2003), and mushrooms (Onem & Nadaroglu, 2014;Onem et al, 2016). The literature on the enzyme immobilization, and the use of different matrices, has been extensively discussed (Mosbach, 1971;Mateo et al, 2007;Spahn & Minteer, 2008;Liu et al, 2018;Sastre et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

“…The literature on the enzyme immobilization, and the use of different matrices, has been extensively discussed (Mosbach, 1971;Mateo et al, 2007;Spahn & Minteer, 2008;Liu et al, 2018;Sastre et al, 2020). Immobilized phytase has more comprehensive applications, like use as amperometric biosensor for the detection of phytate (Moraes et al, 2008) as fertilizer, and as a source of exogenous Pi (Trouillofou et al, 2015), as feed (Cho et al, 2011;Coutinho et al, 2020), as bioreactors (Greiner & Konietzny, 1996), and reduction of phytic acid content from soymilk (Chen et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Phytase from Rice Bean (Vigna umbellata Thunb.) on Glutaraldehyde Activated Chitosan Microspheres

Belho¹,

Ambasht²

2021

JSR

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The immobilization of phytase from rice bean was optimized on the glutaraldehyde-activated chitosan microsphere, and characterized. The optimum percent immobilization was 77.48%, when microspheres were prepared with 1.5% chitosan, activated with glutaraldehyde (0.5%, for 4 h) and with the enzyme protein (0.2 mg/mL, and coupling time 4 h). The immobilized phytase exhibited elongated fibres and pores. FTIR results suggest the formation of a Schiff base with a band at 1638 cm-1. The pH and temperature optimum of immobilized phytase was 4.0 and 40 °C, respectively. The energy of activation was 34.5 kJ/mol. The Km and Vmax values of immobilized phytase were 0.62 mM and 3.42 μmol/min. The immobilized enzyme when incubated at 50 °C, retained 59% activity after 75 min. The immobilized phytase showed 80% activity retention, after 14 days, when stored at 4 °C. The immobilized phytase could be reused for 4 cycles with 58% activity retention. The immobilized phytase, when incubated for 60 min in the presence trypsin and pepsin, showed 92.9 and 95% activity retention, respectively. The properties of immobilized phytase did not alter with respect to pH, and temperature optima. Immobilized phytase exhibited proteolytic resistance when incubated with pepsin for 1 h, and this can find application in animal feed.

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Phytase Immobilization on Hydroxyapatite Nanoparticles Improves Its Properties for Use in Animal Feed

Cited by 33 publications

References 55 publications

Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Zeolite-based nanocomposite as a smart pH-sensitive nanovehicle for release of xylanase as poultry feed supplement

Immobilization of Phytase from Rice Bean (Vigna umbellata Thunb.) on Glutaraldehyde Activated Chitosan Microspheres

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Phytase Immobilization on Hydroxyapatite Nanoparticles Improves Its Properties for Use in Animal Feed

Cited by 33 publications

References 55 publications

Hydroxyapatite-CoFe2O4 Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Hydroxyapatite-CoFe2O4 Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Zeolite-based nanocomposite as a smart pH-sensitive nanovehicle for release of xylanase as poultry feed supplement

Immobilization of Phytase from Rice Bean (Vigna umbellata Thunb.) on Glutaraldehyde Activated Chitosan Microspheres

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Product

Resources

About

Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery

Hydroxyapatite-CoFe₂O₄ Magnetic Nanoparticle Composites for Industrial Enzyme Immobilization, Use, and Recovery