Dimethyl sulphoxide as a solvent for amylose in the determination of amylolytic activity

Griffin, Patrick J.; Fogarty, William M.

doi:10.1002/jctb.5020230406

J. Appl. Chem.

1973

DOI: 10.1002/jctb.5020230406

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Dimethyl sulphoxide as a solvent for amylose in the determination of amylolytic activity

Patrick J. Griffin

William M. Fogarty

Abstract: Amylose readily dissolves in dimethyl sulphoxide (DMSO) to give clear colourless solution which is stable and forms a convenient stock amylose solution for amylase determinations. Dimethyl sulphoxide has no inhibitory effect on different amylolytic enzymes at the concentrations required for enzyme assay.

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1973

1985

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Cited by 13 publications

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Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides

Lenders

Crichton

1984

Biotech & Bioengineering

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The immobilization of pullulanase and beta-amylase on soluble polysaccharides (dextrans and amylose) has been carried out. The method used for coupling the enzymes to the carbohydrate support involves limited periodate oxidation of the polysaccharide followed by reductive alkylation with sodium cyanoborohydride or borohydride. The influence of the degree of functionalization of the carbohydrate, the incubation time, the nature of the reducing agent and, for the dextrans studied, their molecular weight, on the properties of the conjugate were studied. We have observed an apparent correlation between the molecular weight of the glycoprotein conjugates formed and their thermal stability, resistance to urea denaturation and their kinetic parameters. By selecting the proper experimental conditions leading to conjugates with maximum thermal stabilities, it has also been shown that beta-amylase conjugates can hydrolyze starch at a temperature 20 degrees C higher than the corresponding value for the native enzyme. This result demonstrates that conjugation may result in modified enzymes leaving a high operational stability at elevated temperatures. We suggest that the immobilization method presented in this article represents an approach to the stabilization of enzymes employed at an industrial level, which may be of general application.

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Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides

Lenders

Crichton

1984

Biotech & Bioengineering

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Immobilization of a soluble chemically thermostabilized enzyme

Lenders

Germain

Crichton

1985

Biotech & Bioengineering

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Cellobiase was coupled to a dialdehyde dextran by reductive alkylation in the presence of sodium cyanoborohydride. The resulting conjugate, obtained without loss of enzymic activity, presents properties of thermoresistance largely superior to those of native enzyme: the rate of inactivation is reduced compared to that of native enzyme and its optimal temperature of activity is 70-75 degrees C instead of 65 degrees C. Finally the conjugate presents increased longevity when subjected to experiments of operational stability; its hydrolytic activity is maintained at 60 degrees C in a 10% (w/v) cellobiose solution for more than 100 h whereas the native enzyme is inactivated after 45 h. The cellobiase-dextran conjugate was immobilized by covalent coupling on aminated silica by reductive alkylation in the presence of NaBH(3)CN. The characteristics of thermoresistance of this stabilized and immobilized conjugate were studied and compared to those of a preparation of native cellobiase immobilized on a silica support activated with glutaraldehyde. Analysis of the thermoresistance of these two cellobiase preparations clearly shows that immobilization has maintained and even enhanced their properties. In particular, the operational stability, measured at 68 degrees C on 10% (w/v) cellobiose shows an increased longevity of the stabilized and immobilized enzyme for 120 h compared to 60 h for the native immobilized enzyme. Two successive incubations of these cellobiase derivatives show that it is possible to obtain 2.5 times more glucose with the stabilized-immobilized enzyme than with the immobilized preparation. The procedure described above enables us to prepare a thermostabilized immobilized cellobiase.

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Production and purification of a maltose‐producing amylase from Bacillus subtilis IMD 198

Fogarty

Bourke

1983

J. Chem. Technol. Biotechnol.

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A strain of Bacillus subtilis (IMD 198) isolated from peat degraded starch to maltose with little production of glucose and other products. Highest levels of enzyme were achieved in a salts medium containing soya bean meal and starch. The enzyme was purified by precipitation with isopropanol, adsorption on calcium phosphate gel and fractionation on DEAE‐and CM‐cellulose ion‐exchange resins. The latter chromatographic procedure removed a contaminating activity that produced dextrins as end‐products from starch or amylose. The action pattern of the purified, major enzyme activity indicates that it may be β‐amylase.

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Dimethyl sulphoxide as a solvent for amylose in the determination of amylolytic activity

Cited by 13 publications

References 13 publications

Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides

Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides

Immobilization of a soluble chemically thermostabilized enzyme

Production and purification of a maltose‐producing amylase from Bacillus subtilis IMD 198

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