Preparation and functional properties of trypsin modified by carboxymethylcellulose

Villalonga, Reynaldo; Villalonga, María L.; Gómez, Leissy

doi:10.1016/s1381-1177(00)00003-5

Cited by 79 publications

(59 citation statements)

References 37 publications

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“…Recently, this laboratory reported that the modi®cation of hydrolytic enzymes by carboxymethylcellulose improved stability to these biocatalysts under various denaturing conditions. 4,5 In general, glycoenzymes are resistant to covalent modi®cation with macromolecular supports, due to masking of the side-chain reactive groups from the protein by oligosaccharide chains. 6 On the other hand, carbohydrate moieties are not generally involved in functional activity of glycoenzymes.…”

Section: Introductionmentioning

confidence: 99%

Functional stabilization of cellulase by covalent modification with chitosan

Darias

Villalonga

2001

J of Chemical Tech & Biotech

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Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate-activated carbohydrate moieties of the enzyme. The modi®ed enzyme contained about 1.5 mol of polymer per mol of protein. The speci®c activity of the conjugate prepared was 39.8% of the native cellulase. The optimum pH and temperature for cellulase remained unaltered after modi®cation. The thermostability was increased by 8.9°C for the cellulase±chitosan complex. Thermal inactivation at different temperatures ranging from 65°C to 80°C was markedly increased for the polymer-modi®ed enzyme. The stability within the pH range 1.0±3.2 was also improved for the modi®ed enzyme.

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Section: Introductionmentioning

confidence: 99%

Functional stabilization of cellulase by covalent modification with chitosan

Darias

Villalonga

2001

J of Chemical Tech & Biotech

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“…Vacuum-dried Sepharose (1.0 g) was directly incubated with epichlorohydrin and stirred on a magnetic stirrer at 100 rpm at 25 C for 4 h. Epoxyactivated Sepharose was then recovered by centrifugation at 4,000 rpm for 10 min at 8 C and washed with acetone and water. The product was air dried at 8 C and stored at room temperature as ASp.…”

Section: Methodsmentioning

confidence: 99%

Immobilization of Lipase on Epoxy Activated (1→3)-α-D-Glucan Isolated fromPenicillium chrysongenum

Wang¹,

Li²,

Nie³

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…4 Chemical crosslinking of enzymes with polyactivated macromolecules have been extensively used as a method for stabilizing such kind of catalysts. [5][6][7][8] Through this approach the catalytic and functional activity of several enzymes have been improved. [5][6][7][8] However, the adducts prepared showed undefined chemical structure and in some case lower catalytic behavior.…”

Section: Introductionmentioning

confidence: 99%

“…[5][6][7][8] Through this approach the catalytic and functional activity of several enzymes have been improved. [5][6][7][8] However, the adducts prepared showed undefined chemical structure and in some case lower catalytic behavior. 9 For this reason, the development of alternative modification methods for preparing pharmacologically active polymer-protein conjugates with more defined composition receives considerable attention in pharmacological sciences.…”

Section: Introductionmentioning

confidence: 99%