Laccase stabilization by covalent binding immobilization on activated polyvinyl alcohol carrier

Diao, Yinghui; Wang, Qiuling; Fu, Shiyu

doi:10.1046/j.1472-765x.2002.01196.x

Cited by 52 publications

(28 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Upon repeated uses, either blocking of some pores of semi-IPNs by substrate or product may take place, or enzyme may lose its activity and denatures. In literature, the retained activity after 10 batch uses was reported as 60% for covalently immobilized laccase on activated poly(vinyl alcohol) (Yinghui et al, 2002). Thus the results of this study are comparable with those reported in the literature.…”

Section: Ph Temperature and Operational Stabilities Of Immobilized Lsupporting

confidence: 90%

Immobilization of laccase in κ-carrageenan based semi-interpenetrating polymer networks

Makas

Kalkan

Aksoy

et al. 2010

Journal of Biotechnology

View full text Add to dashboard Cite

Section: Ph Temperature and Operational Stabilities Of Immobilized Lsupporting

confidence: 90%

Immobilization of laccase in κ-carrageenan based semi-interpenetrating polymer networks

Makas

Kalkan

Aksoy

et al. 2010

Journal of Biotechnology

View full text Add to dashboard Cite

“…With the exception of AgRSDA-CROSS, modified RSDA exhibited lower activity at pH below pH 5.0. Similar results were observed for amylase immobilized on chitosan (Tripathi et al 2007), pectinase from A. niger immobilized on polyacrylonitrile membrane (Delcheva et al 2007), gelatin entrapped agalactosidase (Naganagouda et al 2007) and laccase immobilized by covalent binding on polyvinyl alcohol carrier (Yinghui et al 2002). The activity of PGAg-RSDA, GAg-RSDA, GlyAg-RSDA and AgRSDA-CROSS shifted towards the basic side to varying degrees.…”

Section: Immobilization On Ph Activity and Stabilitysupporting

confidence: 73%

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

View full text Add to dashboard Cite

Applications of raw starch digesting amylases (RSDAs) are limited due to instability, product inhibition of enzyme and contamination. RSDA from Aspergillus carbonarius was stabilized through immobilization on agarose gel by adsorption, spontaneous crosslinking and conjugation using glycidol, glutaraldehyde or polyglutaraldehyde. Effects of immobilization on kinetics, catalytic, storage and operational stability of immobilized enzyme were evaluated. Polyglutaraldehyde activated agarose RSDA (PGAg-RSDA) gave the highest immobilization yield (100%) with expressed activity of 86.7% while that of glycidol activated RSDA (GlyAg-RSDA) was 80.4%. A shift in pH from optimum of 5 for the soluble enzyme to 6 for RSDA adsorbed on agarose followed by crosslinking with glutaraldehyde (AgRSDA-CROSS) and simultaneous adsorption and crosslinking (AgRSDA-RET), and pH 7 for PGAg-RSDA was seen. PGAg-RSDA and AgRSDA-CROSS were most pH stable and retained over 82% of their activities between pH 3.5 and 9 compared to 59% for the soluble enzyme. Thermoinactivation studies showed that immobilized RSDAs with the exception of GAg-RSDA retained over 90% of their activities at 60°C for 120 min while soluble enzyme retained only 76% activity under the same condition. AgRSDA-CROSS, PGAg-RSDA, Gly-RSDA and GAg-RSDA retained approximately 100% of their activities after 30 days storage at 4°C. GlyAg-RSDA retained 99.6%, PGAg-RSDA 94%, AgRSDA-CROSS 90%, GAg-RSDA 86.5% and Ag-RSDA-RET 80% activity after 10 batch reactions. Immobilization stabilized RSDA and permits processing at higher temperatures to reduce contamination.

show abstract

“…However, immobilised laccase retained 65% of initial activity after 10 batches. In literature, laccase immobilised on activated poly(vinyl alcohol) retained 60% of the initial activity values after 10 cycles (Yingui et al 2002), while laccase immobilised on amineterminated magnetic nanocomposites, 80% after five consecutive operations (Xiao et al 2006). …”

Section: Reusability Of the Immobilised Laccasementioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

View full text Add to dashboard Cite

Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

show abstract

Laccase stabilization by covalent binding immobilization on activated polyvinyl alcohol carrier

Cited by 52 publications

References 20 publications

Immobilization of laccase in κ-carrageenan based semi-interpenetrating polymer networks

Immobilization of laccase in κ-carrageenan based semi-interpenetrating polymer networks

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Contact Info

Product

Resources

About