• The Korean Journal of Food And Nutrition
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• v.2 no.2
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• pp.14-20
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• 1989

A strain of Saccharomyces cerevisiae BY-366 was isolated to produce a strong sucrose-hydrolyzing enzyme. After entrapment of yeast cell invertase with alginate, enzymatic properties of immobilized cells were investigated. The results are as follows. 1. The optimum pH of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, and pH stability of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, respectively. 2 Activation energy of immobilized cells was 4.7 kcal/mol. 3 The immobilized preparation exhibited high resistance to heat and urea Induced denaturation. 4, The bead size less than 2 mm in diameter was desirable. 5. In spite of repeated use, the enzyme activity of immobilized cells was inhibited slightly in batch reaction, and a small column of the immobilized preparation could hydrolyze relatively high concentration of sucrose almost quantitatively to more than 6 days.

• Korean Journal of Microbiology
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• v.26 no.2
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• pp.122-128
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• 1988

The enzymatic properties of soil cellobiohydrolase were examined and compared with those of cellobiohydrolase-active extracts from soil in the forms of enzyme-humic complex and humicfree enzyme, and cellobiohydrolase partially pruified from Aspergillus niger. The pH optima of soil cellobiohydrolase and cellobiohydrolase-humic complex were greater by 1.5-3.0 pH units than those of cellobiohydrolase in humic-free extract and from A. niger. Soil cellobiohydrolase and cellobiohydrolase-humic complex were remarkably resistant to thermal denaturation and proteolysis. These results confirm that cellobiohydrolase in soil is atable in conditions which rapidly inactivate microbial cellobiohydrolase and that its stability is due to the immobilization of this enzyme by association with humic substances. The Michaelis-Menten constants (Km) for soil, cellobiohydrolase-humic complex, humic free extract and cellobiohydrolase from A. niger were 22.1mg/ml, 11.3mg/ml, 10.6mg/ml and 4.5 mg/ml of Avicel, respectively.

• Textile Coloration and Finishing
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• v.8 no.3
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• pp.59-65
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• 1996

Cotton fabrics were treated by low temperature plasma and/or cellulase, and its physical and dyeing properties were investigated. All the pretreatments of the cotton with low temperature plasma of oxygen, nitrogen and argon slowed down the rate of weight loss of cotton in cellulase solution. Plasma pretreatment did not show any strength retention effect on cotton fiber in the subsequent cellulase treatment. Pretreatment of cotton with low temperature oxygen plasma decreased the rate of dyeing in direct dye bath, while cellulase or plasma/cellulase pretreatment increased the rate. Equilibrium dye uptake of cotton was not changed greatly by the pretreatments except the normal untreated cotton showed more or less high uptake. The pretreatment of cellulase with a water-soluble carbodiimide reduced the enzymatic activity, and did not show any strength retention of cotton in enzymatic weight loss.

• KSBB Journal
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• v.6 no.2
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• pp.157-166
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• 1991

The structural properties of cellulose are significantly changed with the progress of hydrolysis reaction. The effects of changes on such properties of cellulosic substrate as crystallinity, amicessibility of enzyme to the active site of cellulose surface, and particle size on the kinetics of enzymatic hydrolysis have been studied. Among those physical studies, the apparent surface active site of cellulose particle was found to have the most significant effect on the hydrolysis kinetics. Based on the experimental results, the adsorption affinity of enzyme and hydrolysis rate were mainly influenced by the surface roughness of cellulose particle. The extent of accesssible active site may be expressed as the change of particle diameter. The Langmuir isotherm was proposed in terms of enzyme activity to explain the actual action of enzyme protein.

• Food Science and Biotechnology
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• v.17 no.6
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• pp.1289-1293
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• 2008

Fresh egg yolk (EY) was enzymatically modified using phospholipase $A_2$ ($PLA_2$) to produce an enzymatically modified-egg yolk powder (EM-EYP). The EM-EYP offered significantly higher emulsifying activity, emulsion stability, protein solubility, and mayonnaise stability than the control EYP. By employing $PLA_2$ in the enzymatic modification process, structural changes occurred in the phospholipids and lipoproteins of the yolk, and cleavage of apo-high density lipoprotein (HDL) components (Mw 105 kDa) was detected by sodium dodecyl sulfate-polyaerylamide gel electrophoresis (SDS-PAGE). Based on its functional properties, EM-EYP has great potential as a replacement for fresh EY in the production of processed food products such as mayonnaise.

• Proceedings of the Korean Society of Life Science Conference
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• 2005.04a
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• pp.77-77
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• 2005

• Proceedings of the Korean Society of Life Science Conference
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• 2005.04a
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• pp.78-78
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• 2005

• Proceedings of the Korean Society of Life Science Conference
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• 2003.05a
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• pp.127-127
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• 2003

• Proceedings of the Korean Society of Life Science Conference
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• 2003.10a
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• pp.130-130
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• 2003

• Proceedings of the Korean Society of Life Science Conference
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• 2003.10a
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• pp.131-131
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• 2003