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KMID : 1160620000050040200
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Preventive Nutrition and Food Science
2000 Volume.5 No. 4 p.200 ~ p.204
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Improving the Surface Functionality of Curdlan by Conjugation with Unfolding Protein through Naturally Occurring Maillard Reaction
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Nakamura Soichiro
Ogawa Masahiro
Saeki Hiroki
Saito Masayoshi
Miyasaka Satoko
Hata Junya
Adachi Naoko
Hwang Jae-Kwan
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Abstract
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Protein conjugation of curdlan belonging to β-1,3-glucan was carried out to improve its surface functionalities. The glucan was mixed with phosvitin, α_s-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and the resulting powder was incubated at 60℃ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. Conjugation with unfolding proteins, i.e., phosvitin and α_s-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbumin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the α_s-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and α_s-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
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KEYWORD
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curdlan, solubility, emulsifying properties, unfolding protein, Maillard-type conjugation
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