Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Awad, Ghada E. A.; Esawy, Mona A.; El-Gammal, Eman W.; Mostafa, Hanan; Elnashar, Magdy M. M.; Atwa, Nagwa A

doi:10.4103/1687-4315.161268

Cited by 12 publications

(8 citation statements)

References 16 publications

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“…At higher temperatures, the microspheres tend to become softer, as the incubation time is also 30 min. In some cases, the immobilized enzyme had a higher temperature optimum, in comparison to the free enzyme (Liu et al, 1999;In et al, 2007;Awad et al, 2015).…”

Section: Effect Of Ph and Temperature On Free And Immobilized Phytasementioning

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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Section: Effect Of Ph and Temperature On Free And Immobilized Phytasementioning

confidence: 99%

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

Belho¹,

Ambasht²

2021

JSR

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“…phytase is used as food/feed additive for its special effect on mineral deficiency elimination, potential effect in the blood clots, cholesterol, and triglycerides reduction, heart diseases prevention [28]. Practical application of phytase is generally restricted by their short life time and stability [8]. One of the essential factor for biocatalysts such as phytase is their stability.…”

Section: Effect Of Nano-particles On Enzyme Activitymentioning

confidence: 99%

“…Phytase has been reported to be immobilised on many kinds of supports, e.g. alginate/carrageenan beads [8] and magnetite chitosan nanoparticles [9] but there is still the need for further development in selecting the efficient support. Supports can be classified as inorganic and organic according to their chemical composition.…”

Section: Introductionmentioning

confidence: 99%

Immobilisation of phytase producing Gluconacetobacter with bacterial cellulose nano‐fibres and promotion of enzyme activities by magnetite nanoparticles

Tabaii

Chatraei

Emtiazi

2018

IET nanobiotechnol.

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The isolated Gluconacetobacter sp. with accession number: KY996741 was assayed for evaluation of phytase activity. It could solubilise sodium phytate in the absence of soluble phosphate with the cells; however, the enzyme was not seen in cell free extract, to the best of their knowledge the intracellular phytase activities of Gluconacetobacter sp. was not reported previously. Also, the potential of in situ immobilisation of cells produced enzyme (/phytase producing bacteria) in bacterial cellulose was investigated and was studied by SEM and AFM. The results showed that the immobilised probiotic cells had the best activity of 1229 U/ml. The optimum temperature of the immobilised enzyme activity was at 45°C (5969 U/ml) and the immobilised phytase maintained 64% of its activities after two repeated cycles. The enzyme needs mild conditions for its activity and has a short life time and low stability and lost activities from 1229 to 500 U/ml during 30 days. However, it was showed that the addition of 1 ppm nano-ferric oxide particles could promote the phytase activities of immobilised cell from 500 U/ml to >1500 U/ml. This immobilised phytase producing cells on bacterial cellulose can be useful as food and/feed supplement for phytin removal.

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“…Starch agar beads have been utilized successfully for immobilization of E. coli for phytase production (Kuek 1991). Conidiospores of S. thermophile (Singh and Satyanarayana 2008) and P. purpurogenu GE1 (Awad et al 2015) immobilized in alginate and carrageenan were used for phytase production, respectively. Ca-alginate immobilized C. krusei cells (Quan et al 2003) and sporangiospores of T. indicae-seudaticae (Kumar and Satyanarayana 2007) have been used successfully for phytase and glucoamylase production, respectively.…”

Section: Immobilization Of Conidiospores For Phytase Productionmentioning

confidence: 99%

“…Immobilization of permeabilized P. anomala cells in alginate showed reusability with sustained phytase activity (Kaur and Satyanarayana 2010). Aspergillus phoenicus produced sustainable glucoamylase over five sequential batches (Awad et al 2015), while T. indicae- seudaticae secreted sustainable glucoamylase titres up to eight repeated batch fermentations (Kumar and Satyanarayana 2007).…”

Section: Immobilization Of Conidiospores For Phytase Productionmentioning

confidence: 99%

Free and immobilized Aspergillus oryzae SBS50 producing protease-resistant and thermostable phytase

Sapna

Singh

2017

3 Biotech

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Optimization for enhanced phytase production by Aspergillus oryzae SBS50 in submerged fermentation was investigated using Taguchi design. In first step design, starch, beef extract, magnesium sulphate, ferrous sulphate and Tween 80 were identified as significant factors affecting phytase production. These significant factors were further optimized at four different levels using a second Taguchi design and were observed that 1% starch, 2% beef extact, 3% Tween 80, 0.1% magnesium sulphate and 0.225% ferrous sulphate supported maximum phytase production (47,432 U/L). The use of Taguchi designed experiments resulted in 14.9-fold enhancement in phytase production compared to the medium optimized by 'one variable at a time' approach. Furthermore, 4% agar immobilized conidiospores of A. oryzae supported high phytase production compared with free cells and other matrices. Agar-immobilized conidiospores resulted in sustained phytase production up to eight repeated batch cycles followed by a decrease in enzyme titres.

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Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Cited by 12 publications

References 16 publications

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

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

Immobilisation of phytase producing Gluconacetobacter with bacterial cellulose nano‐fibres and promotion of enzyme activities by magnetite nanoparticles

Free and immobilized Aspergillus oryzae SBS50 producing protease-resistant and thermostable phytase

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