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        검색결과 5

        4.
        2006.06 KCI 등재 서비스 종료(열람 제한)
        Cheese analogs using lipoxygenase-defected soymilk and α -chymotrypsin modified soy protein isolate (SPI) were prepared. Color, textural properties, sensory attributes and melting spreadability of cheese analogs were evaluated and compared with mozzarella cheese, and relationships between textural properties, sensory attributes and melting spreadability of cheese analogs were analyzed. Off-flavors were not mostly discriminated. Cheese analogs containing 10% SPI untreated and containing 6% and 8% SPI treated by α -chymotrypsin in δE value of color were the most similar to mozzarella cheese. Quality characteristics and melting spreadability of cheese analogs were highly affected and improved by α -chymotrypsin modification. Sensory attributes and melting spreadability of cheese analogs containing 6% SPI treated by α -chymotrypsin were the most similar to mozzarella cheese, while in textural properties, cheese analogs containing 10% SPI were the most similar with mozzarella cheese. Hardness in sensory attributes was highly positively correlated with hardness (r>0.65), adhesiveness (r>0.56), chewiness (r>0.77) and gumminess (r>0.76) in textural properties, while it was highly negatively correlated with melting spreadability (r>-0.68).
        5.
        2006.06 KCI 등재 서비스 종료(열람 제한)
        Effects of α -chymotrypsin modification on degree of hydrolysis (DH), solubility, emulsifying capacity and thermal aggregation of laboratory-purified soy protein isolate (SPI) using a lipoxygenase-defected soybean (Jinpum-kong) and commercial soy protein isolate (Supro 500E) were compared. SPIs were hydrolyzed by α -chymotrypsin at pH 7.8 and 37~circC for 30 min. DHs of Supro 500E and Jinpum-kong SPI were increased by α -chymotrypsin modification, and DH of Supro 500E was higher than that of Jinpum-kong SPI. DH of α -chymotrypsin treated Jinpum-kong SPI was similar with untreated Supro 500E and DH of treated Supro 500E was the highest. Solubility, emulsifying capacity and thermal aggregation of SPIs were increased by α -chymotrypsin modification, and these changes were highly related to changes in DH. Functional properties of Supro 500E were higher than Jinpum-kong SPI in both of untreated and α -chymotrypsin treated SPIs.