Entrapment of α-amylase in alginate beads: Single step protocol for purification and thermal stabilization

Kumar, R. Siva Sai; Kurawattimath, Vishwanath; Singh, Sridevi Annapurna; Rao, A. G. Appu

doi:10.1016/j.procbio.2006.05.028

Cited by 49 publications

(35 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, the molecular weight of amylase differs depending on different origins, species, and development stages of the plants. The results of our experiment that examined pH optimum for the purified amylase activity were similar to those of the other studies which showed the optimum pH to be between 5.0 and 6.0: the amylase of Termitomyces clypeatus had an optimum pH of 5.5 (Ghosh & Sengupta, 1987); the amylase of Eleusine clypeatus, pHs 5.0-5.5 (Nirmala & Muralikrishna, 2003); the b-amylase of soybean, pHs 5-6 (Gertler & Birk, 1965;Kumar, Vishwanath, Singh, & Rao, 2006); and the amylase in fermented cassava flour, pH 6.0 (Ganiyu, 2005). However, two acidic a-amylases of Bacillus stearothermophilus exhibited pH optimum at 4.5 and 5.0, respectively.…”

Section: Discussionsupporting

confidence: 87%

Purification of soybean amylase by superparamagnetic particles

Lin

Kuo

et al. 2009

Food Chemistry

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 87%

Purification of soybean amylase by superparamagnetic particles

Lin

Kuo

et al. 2009

Food Chemistry

View full text Add to dashboard Cite

“…The midpoint of the thermal inactivation for the enzyme increased by 6±1°C upon entrapment. The reusability of the beads was dependent on the bead size and could be reused for six cycles with ∼30% loss in activity (27).…”

Section: Discussionmentioning

confidence: 99%

Stability Improvement of Immobilized a-amylase using Nano Pore Zeolite

et al. 2016

View full text Add to dashboard Cite

“…(Baskar, Banu, Leuca, Gayathri, & Jeyashree, 2015) studied amylase immobilization on magnetic nanoparticles and residual activity of 75% after five times of use. Another study reported that alpha-amylase immobilized using Caalginate could be used six times of use and loss of activity of about 30% (Kumar, Vishwanath, Singh, & Rao, 2006). (Ahmad et al, 2010) did immobilization of glucose oxidase method using Ca-alginate entrapment and residual activity amounted to 47.06% after the fourth reaction cycle.…”

Section: Introductionmentioning

confidence: 99%

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

Zusfahair

Ningsih

Kartika

et al. 2017

Molekul

View full text Add to dashboard Cite

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...

show abstract

Entrapment of α-amylase in alginate beads: Single step protocol for purification and thermal stabilization

Cited by 49 publications

References 23 publications

Purification of soybean amylase by superparamagnetic particles

Purification of soybean amylase by superparamagnetic particles

Stability Improvement of Immobilized a-amylase using Nano Pore Zeolite

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

Contact Info

Product

Resources

About