Phytate degradation by immobilizedSaccharomyces cerevisiae phytase in soybean-curd whey

In, Man-Jin; Kim, Kyung‐Hee; Oh, Nam-Soon

doi:10.1007/bf02931055

Cited by 10 publications

(7 citation statements)

References 19 publications

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“…The pH optimum of the immobilized enzyme was at pH 4.0, like that of free enzyme, without any shift. Our results are consistent with some other reports, where no shift in pH optimum has been reported (Liu et al, 1999;In et al, 2007;Celem & Onal, 2009b;Trouillefou et al, 2015). Further, it is evident that the immobilized enzyme showed higher activity at any pH value.…”

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

confidence: 93%

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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 Phytasesupporting

confidence: 93%

“…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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“…Immobilization yield of the phytase reached 43%. [40] Substrate specificity Substrate specificity of the immobilized phytase was tested on sodium phytate, 4-methylumbelliferil phosphate, glucose 6-phosphate, ADP, and ATP. Chitosan-immobilized enzyme exhibited broad substrate specificity and was more active to hydrolyze sodium phytate (Table 1).…”

Section: Resistance Of Immobilized Enzymes To Proteolysismentioning

confidence: 99%

“…[41] The optimum pH for immobilized Saccbaromyces cerevisiae CY phytases in soybean curd whey was determined as 3.5. [40] A concentrated extract from soybean sprout containing an active phytase was immobilized on Sepabead EC-EP, and the optimum pH of immobilized enzyme was found as 5.0. [37] The pH stability of the chitosan-immobilized enzyme was determined at 4°C, 35°C, and 95°C in the buffer solutions of pH 2.0, 5.0, and 7.0.…”

Section: Optimum Ph and Ph Stability Of Enzymesmentioning

confidence: 99%

Dephytinization of food stuffs by phytase of Geobacillus sp. TF16 immobilized in chitosan and calcium-alginate

Şirin

Akatin

Çolak

et al. 2017

International Journal of Food Properties

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In this work, Geobacillus sp. TF16 phytase was separately immobilized in chitosan and Ca-alginate with the efficiency of 38% and 42%, respectively. These enzymes exhibited broad substrate specificity. Maximal relative phytase activity was measured at pH 5.0 and 95°C and pH 3.0 and 75°C for chitosan and Ca-alginate, respectively. The enzymes were highly stable in a wide pH and temperature range. Values of K m and V max were determined as 2.38 mM and 3401.36 U/mg protein for chitosan, and 7.5 mM and 5011.12 U/mg protein for Ca-alginate. The immobilized enzymes showed higher resistance to proteolysis. After 4 h incubation, hydrolysis capacities of chitosan-and Ca-alginate immobilized enzymes for soymilk phytate were calculated as 24% and 33%, respectively. The chitosan-and Ca-alginate immobilized phytases conserved its original activity after 8 and 6 cycles of reuse, respectively. The features of the enzymes were very attractive and they might be useful for some industrial applications.

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“…In order to minimize the cost of immobilization, use of an anion exchanger like DEAE cellulose is reported [9]. Use of immobilized whole yeast cells for phytate degradation has also been reported recently [17].…”

Section: Introductionmentioning

confidence: 99%

Effect of calcium on immobilization of rice (Oryza sativa L.) peroxidase for bioassays in sodium alginate and Agarose gel

Nahakpam

Singh

Shah

2008

Biotechnol Bioproc E

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The direct immobilization of soluble peroxidase isolated and partially purified from shoots of rice seedlings in calcium alginate beads and in calcium agarose gel was carried out. Peroxidase was assayed for guaiacol oxidation products in presence of hydrogen peroxide. The maximum specific activity and immobilization yield of the calcium agarose immobilized peroxidase reached 2,200 U mg −1 protein (540 mU cm −3 gel) and 82%, respectively. In calcium alginate the maximum activity of peroxidase upon immobilization was 210 mU g −1 bead with 46% yield. The optimal pH for agarose immobilized peroxidase was 7.0 which differed from the pH 6.0 for soluble peroxidase. The optimum temperature for the agarose immobilized peroxidase however was 30°C, which was similar to that of soluble peroxidase. The thermal stability of calcium agarose immobilized peroxidase significantly enhanced over a temperature range of 30~60°C upon immobilization. The operational stability of peroxidase was examined with repeated hydrogen peroxide oxidation at varying time intervals. Based on 50% conversion of hydrogen peroxide and four times reuse of immobilized gel, the specific degradation of guaiacol for the agarose immobilized peroxidase increased three folds compared to that of soluble peroxidase. Nearly 165% increase in the enzyme protein binding to agarose in presence of calcium was noted. The results suggest that the presence of calcium, ions help in the immobilization process of peroxidase from rice shoots and mediates the direct binding of the enzyme to the agarose gel and that agarose seems to be a better immobilization matrix for peroxidase compared to sodium alginate. © KSBB hÉóïçêÇëW=~Ö~êçëÉI=~äÖáå~íÉI=Å~äÅáìãI=áããçÄáäáòÉÇ=éÉêçñáÇ~ëÉI=Oryza sativaI=éÉêçñáÇ~ëÉ= = = = =

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Phytate degradation by immobilizedSaccharomyces cerevisiae phytase in soybean-curd whey

Cited by 10 publications

References 19 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

Dephytinization of food stuffs by phytase of Geobacillus sp. TF16 immobilized in chitosan and calcium-alginate

Effect of calcium on immobilization of rice (Oryza sativa L.) peroxidase for bioassays in sodium alginate and Agarose gel

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