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논문 기본 정보

자료유형
학술저널
저자정보
Jeong, Ji-Eun (Department of Food and Nutrition, College of Human Ecology. Human Ecology Research Institute, Chonnam National University) Hong, Youn-Ho (Department of Food and Nutrition, College of Human Ecology. Human Ecology Research Institute, Chonnam National University)
저널정보
한국축산식품학회 한국축산식품학회지 한국축산식품학회지 제29권 제4호
발행연도
2009.1
수록면
415 - 422 (8page)

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초록· 키워드

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In this study, several factors were analyzed in an effort to determine the effects of transglutaminase (TGase) treatment on sodium caseinate (NaCN), ${\alpha}--lactalbumin$ (${\alpha}-La$), and ${\beta}-lactoglobulin$ (${\beta}-Lg$) polymerization reactions. The results of SDSPAGE showed that NaCN was slightly hydrolyzed to molecular weights of 50-400 kDa according to activation time. ${\alpha}-La$ formed high-molecular polymers of 30-300 kDa, whereas ${\beta}-Lg$ remained almost completely unhydrolyzed. Melting temperatures of NaCN, ${\alpha}-La$ with and without TGase were all in the range of $100{\pm}10^{\circ}C$ under the endothermic curve, and the melting temperature of ${\beta}-Lg$ with TGase was lower than that with TGase. When the proteins were incubated for 3 h with TGase, the micrographic structures showed a small quantity of sediment and broad layers. The final ${\alpha}-La$ residues remained at a level of 21.38%, and the TGase-treated ${\alpha}-La$ was confirmed to have undergone a profound loss of mass, to 18.25%. The DPPH-radical scavenging activity of NaCN and ${\beta}-Lg$ with TGase treatment was higher than that observed in the untreated sample, while those of ${\alpha}-La$ increased with concentration.

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