Immobilization of starch-converting enzymes on surface-modified carriers using single and co-immobilized systems: properties and application to starch hydrolysis

Park, Dae‐Won; Haam, Seungjoo; Jang, Kyongho; Ahn, Ik Sung; Kim, Woo Sik

doi:10.1016/j.procbio.2003.11.039

Cited by 58 publications

(26 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This decrease in K m value upon immobilization is occasionally occurs in some immobilization works and the decrease in this presented work was calculated approximately as 3.2 fold. K m is the indicator for the affinity of an enzyme towards its substrate [38] and there is an inverse proportion between the value of K m and "affinity". This means that, lower values of K m indicates higher affinity between enzyme and its substrates.…”

Section: Effects Of Ph and Temperaturementioning

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

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

Section: Effects Of Ph and Temperaturementioning

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

View full text Add to dashboard Cite

show abstract

“…However, in the case of our LiP the hyperactivation was much less as compared to Rhizomucor miehei lipase (Aucoin et al 2004) which was activated to more than 200% when entrapped in a hydrophobic xerogel. The hyperactivation may be in part attributable to xerogel-LiP interactions producing a stabilizing affect and leading to the enhanced conformational stability (Park et al 2005). Probably, the LiP underwent a beneficial conformational change in the presence of these hydrophobic sites while being entrapped within the silica network (Reetz et al 1996).…”

Section: Effect Of Immobilization On Lip Activitymentioning

confidence: 99%

Hyperactivation and thermostabilization of Phanerochaete chrysosporium lignin peroxidase by immobilization in xerogels

Asgher¹,

Asad²,

Bhatti³

et al. 2006

World J Microbiol Biotechnol

View full text Add to dashboard Cite

This is a continuation of our previous paper on production of lignin peroxidase (LiP) by Phanerochaete chrysosporium in solid substrate fermentation (SSF) medium of corncobs. The enzyme was purified by ammonium sulphate precipitation and ion-exchange fast protein liquid chromatography. Maximum yield of LiP was 13.7 U/gds (units per gram dry substrate) after 5 days of SSF with 70% moisture and 20% (v/w) inoculum. The approximate molecular mass of purified LiP, estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, was 38 kDa. The pH and temperature optima for the LiP were 4 and 40°C, respectively. Immobilization of LiP in hydrophobic xerogels caused hyperactivation of LiP and enhanced its thermostability properties. The K M and V max values for immobilized LiP were 10.56 mg/ml and 16.67 lmol/ min (120.49 U/mg of protein) as compared to 13 mg/ml and 11.76 lmol/min (85 U/mg of protein), respectively, for free LiP using veratryl alcohol as substrate.

show abstract

“…[19] Therefore, a hydrophilic silica gel was selected as the b-glucanase-immobilized carrier in this study. To determine the appropriate size of silica for immobilization, the effects of three types of b-glucanase-immobilized silica on the hydrolysis of polysaccharides were studied ( Figure 4).…”

Section: Screening Of Silica Size and Optimization Of Hydrolysis Timementioning

confidence: 99%

“…Park et al reported a similar effect of temperature on the hydrolysis of starch using an enzyme on the modified carriers. [19] Effect of the Amount of b-glucanase-Immobilized Silica Figure 6 shows the glucose yield on b-glucanase-immobilized 10-25 mm silica at 40 C for 10 hr. The glucose yield was 7.15, 12.77, and 9.31 mg=mL using 0.05, 0.15, and 0.25 g of enzyme-silica, respectively.…”

Section: Screening Of Silica Size and Optimization Of Hydrolysis Timementioning

confidence: 99%

Effects of β-glucanase-Immobilized Silica on Hydrolysis of Polysaccharides in Chamaecyparis obtusa Residues

Lee

Tang

Zhang

et al. 2014

Journal of Liquid Chromatography & Related Technologies

View full text Add to dashboard Cite

Enzymatic hydrolysis, which is one of the steps in the production of bioethanol, is a major process in the degradation of polysaccharides. Enzyme-immobilized technology has been developed because enzymes can be contaminated easily and are difficult to reuse. In this study, b-glucanase was immobilized on silica, and the effects of the enzyme-silica size, time, temperature, and amount of enzyme-silica on the hydrolysis of polysaccharides in the Chamaecyparis obtusa residue were studied. The enzyme-silica size, time range, temperature, and amount of enzyme-silica studied ranged from 10 to 63 mm, 2 to 12 hr, 25 to 45 C, and 0.05 to 0.25 g, respectively. The optimal enzyme-silica size, time range, temperature, and amount of b-glucanase immobilized on enzyme-silica for the hydrolysis of polysaccharides were found to be 10-25 mm silica, 10 hr, 40 C, and 0.15 g, respectively. The enzyme could not be used at temperatures higher than 40 C due to denaturation. Under the optimal conditions, the glucose yield was 12.77 mg=mL.

show abstract

Immobilization of starch-converting enzymes on surface-modified carriers using single and co-immobilized systems: properties and application to starch hydrolysis

Cited by 58 publications

References 16 publications

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

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

Hyperactivation and thermostabilization of Phanerochaete chrysosporium lignin peroxidase by immobilization in xerogels

Effects of β-glucanase-Immobilized Silica on Hydrolysis of Polysaccharides in Chamaecyparis obtusa Residues

Contact Info

Product

Resources

About