Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: Analytical applications

Kumar, Sandeep; Dwevedi, Alka; Kayastha, Arvind M.

doi:10.1016/j.molcatb.2008.12.006

Cited by 112 publications

(63 citation statements)

References 42 publications

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“…At 1% alginate concentration, esterase may leak out of beads due to soft, unstable and flaccid beads formation during immobilization [18]. The decrease in activity of entrapped esterase using more than 3% alginate concentration during bead formation could be explained as diffusion limitation of substrate in to entrapped enzyme [19]. Therefore, 2% alginate concentration was selected in our studies.…”

Section: Optimum Conditions For Esterase Immobilizationmentioning

confidence: 99%

Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties

Gülay

Şanlı‐Mohamed

2012

International Journal of Biological Macromolecules

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a b s t r a c tThermoalkalophilic esterase enzyme from Balç ova (Agamemnon) geothermal site were aimed to be immobilized effectively via a simple and cost-effective protocol in silicate coated Calcium alginate (Caalginate) beads by entrapment. The optimal immobilization conditions of enzyme in Ca-alginate beads were investigated and obtained with 2% alginate using 0.5 mg/ml enzyme and 0.7 M CaCl 2 solution. In order to prevent enzyme from leaking out of the gel beads, Ca-alginate beads were then coated with silicate. Enzyme loading efficiency and immobilization yield for silicate coated beads was determined as 98.1% and 71.27%, respectively and compared with non-coated ones which were 68.5% and 45.80%, respectively. Surface morphologies, structure and elemental analysis of both silicate coated and noncoated alginate beads were also compared using Fourier Transform Infrared Spectroscopy (FT-IR) and Scanning Electron Microscope (SEM) equipped with Energy-dispersive X-ray spectroscopy (EDX). Moreover, silicate coated alginate beads enhanced reusability of esterase in continuous processes compared to non-coated beads. The hydrolytic properties of free and immobilized enzyme in terms of storage and thermal stability as well as the effects of the temperature and pH were determined. It was observed that operational, thermal and storage stabilities of the esterase were increased with immobilization.

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Section: Optimum Conditions For Esterase Immobilizationmentioning

confidence: 99%

Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties

Gülay

Şanlı‐Mohamed

2012

International Journal of Biological Macromolecules

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“…These results indicate that the optimum pH for amylase immobilized shifted slightly to the acid side. It has been observed in soybean (Glycine max) after immobilized urease calcium alginate (S. Kumar et al, 2009). In general, the immobilization of certain enzymes in the polycationic support matrix will result in a shift in the acid pH optimum.…”

Section: Determining the Optimum Phmentioning

confidence: 99%

“…The immobilized enzyme in solution can have different optimum pH of the enzyme free state as it moves on a solid matrix. Depending on the surface, and residual charge on the solid matrix and the properties of the immobilized enzyme, pH around the enzyme molecule can change, causing a shift in the optimum pH of the enzyme (S. Kumar et al, 2009). …”

Section: Determining the Optimum Phmentioning

confidence: 99%

“…Alginate can be used as a supporting matrix for enzyme immobilization because of the alginate is an anionic polysaccharide that can form a gel when reacted with divalent cations. Ca 2+ ion is one of the most commonly used for immobilization because of low toxicity (S. Kumar, Dwevedi, & Kayastha, 2009). Alginate has been widely used in research as a matrix supporting immobilization of enzymes including immobilization of the enzyme amylase (Riaz, Qader, Anwar, & Iqbal, 2009), protease , lipase (Bhushan, Parshad, Qazi, & Gupta, 2008), urease (Maharani, Prasetyawan, & Mahdi, 2013) and glucose oxidase (Ahmad, Syaiful, & Patong, 2010) Research on the immobilization of enzymes or cells to enhance the ability of repeated use has been widely applied. )…”

Section: Introductionmentioning

confidence: 99%

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Immobilization and Characterization of Bacillus Thuringiensis HCB6 Amylase in Calcium Alginate Matrix

Zusfahair

Ningsih

Kartika

et al. 2017

Molekul

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Free enzyme in solution react with substrates to result in products which cannot be recovered for reuse. These problems can be overcome to a certain extent by the use of enzyme immobilization method. Immobilized enzymes are more robust and more resistant to condition changes. More importantly, the heterogeneous immobilized enzyme systems allow an easy recovery of both enzymes and products, multiple re-uses of enzymes, and continuous operation of enzymatic processes. Entrapment of enzymes in Ca-alginate is one of the simplest methods of immobilization. The aim of this research was to obtain the optimum condition of the making of immobilized amylase beads using a Ca-alginate bead and to determine its characteristics. The optimization of immobilized amylase beads includes variation of sodium alginates and variations of enzyme contact time with CaCl2. The characterization of immobilized amylase includes determination of optimum substrate concentration, optimum pH, and optimum incubation time as well as amylase stability test. Amylase activity was determined by using dinitro salicylic (DNS) method. The results showed that the optimum immobilized amylase obtained at alginate concentrations of 5% (w/v), contact time of 60 minutes and immobilization efficiency of 67.5%. Furthermore, immobilized amylase showed optimum substrate concentration of 1.5-2.5% (w/v), optimum pH of 6, an optimum incubation time of 20 minutes with the activity of 179.8 U/mL. The KM value for free amylase and immobilized amylases were 0.3 mM and 0.12 mM respectively. Vmax value for free amylase and immobilized amylases were 105.3 U/mL and 10.1 U/mL respectively. Immobilized Amylase can be used up to six times with the residual activity of 52.7%. Keywords: Amylase, Ca-alginate, enzyme immobilization ABSTRAKEnzim dalam keadaan bebas (larutan) dapat bereaksi dengan substrat menghasilkan produk kemudian tidak dapat digunakan kembali. Permasalahan ini dapat diatasi dengan metode amobilisasi enzim. Enzim amobil lebih kuat dan lebih tahan terhadap perubahan keadaan. Sistem heterogen enzim amobil memungkinkan kemudahan recovery antara enzim dan produk, pemakaian enzim secara berulang, dan proses enzimatik secara kontinu. Penjebakan enzim dalam kalsium alginat (Ca-alginat) adalah salah satu metode amobilisasi paling sederhana. Penelitian ini bertujuan untuk memperoleh kondisi optimum pembuatan beads amilase amobil menggunakan matrik Ca-alginat, dan mengetahui karakteristiknya. Optimasi pembuatan beads amilase amobil meliputi variasi konsentrasi natrium alginat dan variasi waktu kontak enzim dengan CaCl2. Karakterisasi amilase amobil meliputi penentuan konsentrasi substrat optimum, pH optimum, waktu inkubasi optimum serta uji kestabilan amilase. Aktivitas amilase ditentukan dengan menggunakan metode asam dinitrosalisilat (DNS). Hasil penelitian menunjukkan kondisi optimum pembuatan beads amilase amobil diperoleh pada konsentrasi alginat 5 % (b/v) dan waktu kontak 60 menit dengan nilai efisiensi amobilisasi sebesar 67,5 %. Amilase amobil mempunyai ak...

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“…animal fodder, oil extraction, bio-diesel production etc. For various industrial applications, enzymes so extracted from leguminous seeds are immobilized onto suitable matrices leading to improvement in physico-chemical properties (Das et al, 1997;Kayastha & Srivastava, 2001;Tripathi et al, 2007;Kumar et al, 2009). Figure 1 (A, B) show immobilized -galactosidase from Pisum sativum onto Amberlite MB150 beads and gold nanoparticles ) being used for lactose hydrolysis at industrial scale.…”

Section: Source Of Various Enzymes Having Industrial Significancementioning

confidence: 99%

Soybean: a Multifaceted Legume with Enormous Economic Capabilities

Dwevedi¹,

Kayastha²

2011

Soybean - Biochemistry, Chemistry and Physiology

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Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: Analytical applications

Cited by 112 publications

References 42 publications

Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties

Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties

Immobilization and Characterization of Bacillus Thuringiensis HCB6 Amylase in Calcium Alginate Matrix

Soybean: a Multifaceted Legume with Enormous Economic Capabilities

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