Co-immobilized enzymes in magnetic chitosan beads for improved hydrolysis of macromolecular substrates under a time-varying magnetic field. 2010

Kun Yang, and Ning-Shou Xu, and Wei Wen Su
Department of Molecular Biosciences & Bioengineering, University of Hawaii, 1955 Eastwest Rd., Agricultural Science 218, Honolulu, HI 96822, United States.

Glucoamylase and alpha-amylase co-immobilized with gamma ferric oxide powders in chitosan beads for consecutive starch liquefaction and saccharification under different magnetic fields was investigated. The chitosan concentration in the beads was found to greatly affect the immobilized enzyme performance. Superior immobilization efficiency and enzyme stability were noted when 2% instead of 4% chitosan was utilized. Using confocal microscopy and scanning electron microscopy, the beads with 2% chitosan were seen to exhibit a more rugged surface topology with more macropores and accommodate more protein near the external surface than with the 4% chitosan beads. An optimum loading ratio between alpha-amylase and glucoamylase exists that gives the highest glucose production, and this ratio varies with the size of the beads. The inclusion of the gamma ferric oxide powders renders the beads magnetically anisotropic and causes them to tumble under a single-phase alternating magnetic field, resulted in increased overall reaction rates. When exposed to a three-phase alternating magnetic field, these beads were stirred vigorously, also leading to enhanced reaction rates. The use of multi-enzyme co-immobilization in magnetic anisotropic chitosan beads may be extended to other practical applications that involve coordinated enzymatic reactions of macromolecular substrates.

UI MeSH Term Description Entries
D008280 Magnetics The study of MAGNETIC PHENOMENA. Magnetic
D008863 Microspheres Small uniformly-sized spherical particles, of micrometer dimensions, frequently labeled with radioisotopes or various reagents acting as tags or markers. Latex Beads,Latex Particles,Latex Spheres,Microbeads,Bead, Latex,Beads, Latex,Latex Bead,Latex Particle,Latex Sphere,Microbead,Microsphere,Particle, Latex,Particles, Latex,Sphere, Latex,Spheres, Latex
D004795 Enzyme Stability The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat. Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D004800 Enzymes, Immobilized Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields. Immobilized Enzymes,Enzyme, Immobilized,Immobilized Enzyme
D005087 Glucan 1,4-alpha-Glucosidase An enzyme that catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of polysaccharide chains with the release of beta-glucose. It is also able to hydrolyze 1,6-alpha-glucosidic bonds when the next bond in sequence is 1,4. 1,4-alpha-Glucosidase, Exo,Amyloglucosidase,Exo-1,4-alpha-Glucosidase,Glucoamylase,gamma-Amylase,Glucoamylase G1,Glucoamylase G2,1,4-alpha-Glucosidase, Glucan,Exo 1,4 alpha Glucosidase,Glucan 1,4 alpha Glucosidase,gamma Amylase
D005290 Ferric Compounds Inorganic or organic compounds containing trivalent iron. Compounds, Ferric
D005976 Glutaral One of the protein CROSS-LINKING REAGENTS that is used as a disinfectant for sterilization of heat-sensitive equipment and as a laboratory reagent, especially as a fixative. Glutaraldehyde,Cidex,Diswart,Gludesin,Glutardialdehyde,Glutarol,Korsolex,Novaruca,Sekumatic,Sonacide,Sporicidin
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000447 Aldehydes Organic compounds containing a carbonyl group in the form -CHO. Aldehyde
D000516 alpha-Amylases Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units. Taka-Amylase A,alpha-Amylase,Alpha-Amylase Bayer,Maxilase,Mégamylase,alpha-1,4-D-Glucanglucanohydrolase,Alpha Amylase Bayer,AlphaAmylase Bayer,Taka Amylase A,TakaAmylase A,alpha 1,4 D Glucanglucanohydrolase,alpha Amylase,alpha Amylases

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