Activity and Stability of Enzymes Incorporated into Acrylic Polymers

Yang, Zhen; Mesiano, Anita J.; Venkatasubramanian, Srikanth; Gross, Susan H.; Harris, J. Milton; Russell, Alan J.

doi:10.1021/ja00122a014

Cited by 109 publications

(69 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this latter case the high stability may be due to the very slight leakage of the immobilized enzyme compared with the former case. 17 Yang et al 18 reported that the enhanced stability of the polymer which incorporated subtilisin may be related to the decreased auto-hydrolysis of the enzyme. …”

Section: Reuse Efficiencymentioning

confidence: 99%

Pullulanase immobilization on natural and synthetic polymers

Dessouki

Issa²,

Atia³

2001

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

This work describes the immobilization of pullulanase onto two different polymers; agarose activated with epichlorohydrin and trichlorotriazine and casein activated with epichlorohydrin, in addition to a synthetic copolymer, butylacrylate±acrylic acid (BuA/AAc). Immobilization by covalent binding yields stable enzyme activity. The operational stability of the free and immobilized enzymes showed that the enzyme immobilized by a crosslinking technique using glutaric dialdehyde (GA) showed poor durability and the relative activity decreased sharply due to leakage after repeated washing, while the enzymes immobilized by covalent bonds resulted in a slight decrease in most cases in the relative activity (around 20%) after being used 10 times. Storage for 4±6 months showed that the free enzyme lost most of its activity, while the immobilized enzyme showed the opposite behavior. Subjecting the immobilized enzymes to doses of g-radiation (0.5±10 Mrad) resulted in complete loss in the activity of the free enzyme at a dose of 5 Mrad, while the immobilized enzymes showed relatively high resistance to g-radiation up to a dose of 5 Mrad. Nuclear Magnetic Resonance ( 1 H NMR) and FTIR measurements were carried out to con®rm the structure of the polymer as well as the immobilization process of the enzyme onto the polymeric carrier. The unique biochemical characteristics, mode of action and utility of the environmentally compatible pullulanase in starch conversion are well known. Using pullulanase with b-amylase in starch sacchari®cation processes can increase maltose yield by 20±25%.

show abstract

Section: Reuse Efficiencymentioning

confidence: 99%

Pullulanase immobilization on natural and synthetic polymers

Dessouki

Issa²,

Atia³

2001

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

“…10 Most immobilization strategies are designed by the covalent linking of a protein to a water-insoluble polymer matrix with the enzyme function performed in aqueous media or water-organic media. 11 The covalent binding method, based on the covalent attachment of protein to water-insoluble matrices, has been the most widespread and one of the most thoroughly investigated approaches to enzyme immobilization. 12,13 Synthetic carriers are the most common supports available for protein immobilization.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of catalase on a novel polymer support, crosslinked polystyrene ethylene glycol acrylate resin: Role of the macromolecular matrix on enzyme activity

Kumar

2005

J of Applied Polymer Sci

View full text Add to dashboard Cite

ABSTRACT:Crosslinked polystyrene ethylene glycol acrylate resin (CLPSER) was developed for the immobilization of the enzyme catalase by the introduction of a crosslinker, O,OЈ-bis(2-acrylamidopropyl) poly(ethylene glycol) 1900 , to styrene. The crosslinker was prepared by the treatment of acryloyl chloride with O,OЈ-bis(2-aminopropyl) poly(ethylene glycol) 1900 in the presence of diisopropylethylamine. The resin was characterized with IR and 13 C-NMR spectroscopy. The catalytic activity of the catalase-immobilized system of CLPSER was compared with divinylbenzenecrosslinked polystyrene, ethylene glycol dimethacrylate crosslinked polystyrene, and 1,4-butanediol dimethacrylate crosslinked polystyrene systems. Crosslink levels of 2, 8, and 20 mol % were evaluated. Among these crosslinked systems, the 2 mol % system was found to be most suitable to support catalytic activity. When a long flexible hydrophilic poly(ethylene glycol) crosslink, introduced between the polystyrene (PS) backbone and functional groups was used for immobilization, the extent of coupling and enzyme activity increased. Depending on the nature of the support, the catalytic activity of the system varied. The hydrophilic CLPSER support was most efficient for immobilization compared to the other PS-based supports.

show abstract

“…Insofar as enzymes are concerned, advantages of immobilized enzymes over their counterparts in solution include enhanced temperature and temporal stability of the biocatalyst and ease of separation from the reaction medium, enabling multiple reuses. A number of templates have been used for enzyme immobilization, such as silica nanotubes (Mitchell et al, 2002), phospholipid bilayers (Chen et al, 1999;Hamachi et al, 1994), self-assembled monolayers (Fang et al, 1996;Mrksich et al, 1995), Langmuir -Blodgett films (Boussaand et al, 1998;Nicolini et al, 1993), polymer matrices (Franchina et al, 1999;Yang et al, 1995), galleries of a-zirconium phosphate (Kumar and McLendon, 1997), mesoporous silicates such as MCM-41 (He et al, 2000), silica nanoparticles (Qhobosheane et al, 2001), and thermally evaporated lipid films (Sastry, 2002;Sastry et al, 2002), each with its characteristic advantages and disadvantages.…”

Section: Introductionmentioning

confidence: 99%

Immobilization and biocatalytic activity of fungal protease on gold nanoparticle‐loaded zeolite microspheres

Phadtare

Vinod

Mukhopadhyay

et al. 2004

Biotech & Bioengineering

View full text Add to dashboard Cite

Gold nanoparticles are excellent biocompatible surfaces for the immobilization of enzymes. However, separation of the gold nanoparticle-enzyme bioconjugate material from the reaction medium is often difficult. In this study, we investigate the assembly of the gold nanoparticles on the surface of the amine-functionalized zeolite microspheres in the formation of zeolite-gold nanoparticle "core-shell" structures and, thereafter, the use of this structure in immobilization of fungal protease. The assembly of gold nanoparticles on the zeolite surface occurs through the amine groups present in 3-aminopropyltrimethoxysilane (3-APTS). The fungal proteases bound to the massive "core-shell" structures were easily separated from the reaction medium by mild centrifugation and exhibited excellent reuse characteristics. The biocatalytic activity of fungal protease in the bioconjugate was marginally enhanced relative to the free enzyme in solution. The bioconjugate material also showed significantly enhanced pH and temperature stability and a shift in the optimum temperature of operation.

show abstract

Activity and Stability of Enzymes Incorporated into Acrylic Polymers

Cited by 109 publications

References 0 publications

Pullulanase immobilization on natural and synthetic polymers

Pullulanase immobilization on natural and synthetic polymers

Immobilization of catalase on a novel polymer support, crosslinked polystyrene ethylene glycol acrylate resin: Role of the macromolecular matrix on enzyme activity

Immobilization and biocatalytic activity of fungal protease on gold nanoparticle‐loaded zeolite microspheres

Contact Info

Product

Resources

About