Concanavalin A immobilized poly(ethylene glycol dimethacrylate) based affinity cryogel matrix and usability of invertase immobilization

Uygun, Murat; Uygun, Deniz Aktaş; Özçalışkan, Emir; Akgöl, Sinan; Deni̇zli̇, Adil

doi:10.1016/j.jchromb.2012.01.014

Cited by 40 publications

(32 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The F. graminearum-immobilized β-fructofuranosidase was able to catalyze a higher number of cycles than Lactobacillus brevis enzyme immobilized in alginate beads (13 cycles) (24) as well as invertase immobilized in monolithic cryogel (10 cycles) (25). On the other hand, the invertase immobilized on cotton thread was able to catalyze 28 cycles (10).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Immobilization of Fusarium graminearum β-d-fructofuranosidase using alternative cellulosic supports: Stabilization and production of fructooligosaccharides

Gonçalves

Jorge²,

Guimarães

2015

Food Sci Biotechnol

View full text Add to dashboard Cite

The extracellular β-D-fructofuranosidase from Fusarium graminearum was immobilized using hydrophilic cotton, filter paper, multipurpose cloth, sugar cane bagasse, string, or gauze as alternative cellulosic supports, or with cyanogen bromide agarose. All derivatives (support+enzyme) showed high capacity for reuse (up to 23 times). The derivatives obtained with multipurpose cloth and string were stable at 60 o C maintaining 80% of their activity for more than 120 min. The filter paper derivative had a halflife (T 50 ) of 27 min at 70 o C. When tested for their pH stability (3.0-9.0), all derivatives were more stable than the free enzyme, especially the cotton derivative. The sugarcane bagasse, string, and filter paper derivatives could efficiently produce fructooligosaccharides (FOS) using sucrose as substrate. According to the retention of enzymatic activity, reuse and stabilities, the filter paper and string were the best alternative supports for β-D-fructofuranosidase immobilization, allowing enzyme stabilization and production of FOS.

show abstract

Section: Resultsmentioning

confidence: 99%

“…The derivative obtained using wood sawdust waste was more stable than the free enzyme, completely retaining its activity at 60 o C for 1 h, while the free enzyme retained only 50% of its activity (25). The recombinant enzyme immobilized on nylon-6 maintained approximately 50% of its activity for 1 h at 40 o C (15).…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Fusarium graminearum β-d-fructofuranosidase using alternative cellulosic supports: Stabilization and production of fructooligosaccharides

Gonçalves

Jorge²,

Guimarães

2015

Food Sci Biotechnol

View full text Add to dashboard Cite

show abstract

“…[14] One of the efficient support materials have been used for applications of immobilized enzyme are cryogels. [25][26][27][28][29] Cryogels are polymeric materials prepared at sub-zero temperatures where almost whole part of solvent (usually water) is frozen and all monomers and initiators are concentrated in small non-frozen phase. In this method, growing ice crystals act as a porogen, which forms systems of interconnected large pore, after melting.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of amyloglucosidase onto macroporous cryogels for continuous glucose production from starch

Uygun

Akduman

Ergönül

et al. 2015

Journal of Biomaterials Science, Polymer Edition

Self Cite

View full text Add to dashboard Cite

Poly(methyl methacrylate-glycidyl methacrylate) [Poly(MMA-GMA)] cryogels were synthesized using monomers of methylmethacrylic acid and epoxy group bearing GMA via radical cryopolymerization technique. Synthesized cryogels were used for the immobilization of amyloglucosidase to the cryogel surface using epoxy chemistry. Characterizations of the free and immobilized amyloglucosidase were carried out by comparing the optimum and kinetic parameters of enzymes. For this, pH and temperature profiles of free and immobilized preparation were studied and, it was found that, optimum pH of enzyme was not change upon immobilization (pH 5.0), while optimum temperature of the enzyme shifted 10 °C to warmer region after immobilization (optimum temperatures for free and immobilized enzyme were 55 and 65 °C, respectively). Kinetic parameters of free and immobilized enzyme were also investigated and Km values of free and immobilized amyloglucosidase were found to be 2.743 and 0.865 mg/mL, respectively. Vmax of immobilized amyloglucosidase was found to be (0.496 µmol/min) about four times less than that of free enzyme (2.020 µmol/min). Storage and operational stabilities of immobilized amyloglucosidase were also studied and it was showed that immobilized preparation had much more stability than free preparation. In the present work, amyloglucosidase immobilized poly(MMA-GMA) cryogels were used for continuous glucose syrup production from starch for the first time. Efficiency of immobilized enzyme was investigated and released amount of glucose was found to be 2.54 mg/mL at the end of the 5 min of hydrolysis. The results indicate that the epoxy functionalized cryogels offer a good alternative for amyloglucosidase immobilization applications with increased operational and thermal stability, and reusability. Also, these cryogels can be used for immobilization of other industrially valuable enzymes beyond amyloglucosidase.

show abstract

“…where Q is the adsorption capacity (mg/g); C e is the equilibrium urease concentration (mg/mL); b and K F are the Langmuir and Freundlich constants, respectively, and n is the Freundlich exponent [12] (see Note 20).…”

Section: Urease Adsorptionmentioning

confidence: 99%

Ni(II) Chelated IDA Functionalized Poly(HEMA-GMA) Cryogels for Urease Adsorption

Uygun

2015

Methods in Molecular Biology

Self Cite

View full text Add to dashboard Cite

Cryogelic support materials have been intensively used for the purification and separation of biomolecules. Cryogels are cheap materials, they can be easily used for different purposes and their chemical and physical stabilities are very high. Cryogels can also be easily functionalized with different type of ligands and are be applicable to different affinity systems. Within these affinity systems, immobilized metal affinity chromatography (IMAC) offers efficient and simple protein purification strategies. IMAC technology has been deeply applied to bioseparations studies. In the present chapter, the preparation of a cryogel support material and the functionalization with the chelating agent iminodiacetic acid (IDA) and the subsequent Ni(II) chelation are described. Characterization techniques and the cryogel preparation method are summarized and urease adsorption studies on the metal chelate cryogel are briefly explained.

show abstract

Concanavalin A immobilized poly(ethylene glycol dimethacrylate) based affinity cryogel matrix and usability of invertase immobilization

Cited by 40 publications

References 38 publications

Immobilization of Fusarium graminearum β-d-fructofuranosidase using alternative cellulosic supports: Stabilization and production of fructooligosaccharides

Immobilization of Fusarium graminearum β-d-fructofuranosidase using alternative cellulosic supports: Stabilization and production of fructooligosaccharides

Immobilization of amyloglucosidase onto macroporous cryogels for continuous glucose production from starch

Ni(II) Chelated IDA Functionalized Poly(HEMA-GMA) Cryogels for Urease Adsorption

Contact Info

Product

Resources

About