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자료유형
학술저널
저자정보
Quan, Tran Hong (Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University) Benjakul, Soottawat (Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University)
저널정보
한국축산식품학회 한국축산식품학회지 한국축산식품학회지 제38권 제1호
발행연도
2018.1
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14 - 25 (12page)

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Chemical compositions, trypsin inhibitory activity, and gelling properties of albumen from duck egg during salting of 30 days were studied. As the salting time increased, moisture content decreased, the salt content and surface hydrophobicity increased (p<0.05). Trypsin inhibitory activity and specific activity were continuously decreased throughout the salting time of 30 days (p<0.05). This coincided with the decrease in band intensity of inhibitor with molecular weight of 44 kDa as examined by inhibitory activity staining. Nevertheless, no differences in protein patterns were observed in albumen during the salting of 30 days. Based on texture profile analysis, hardness, springiness, gumminess, chewiness, and resilience of albumen gel decreased with increasing salting time. Conversely, salted albumen gels exhibited higher cohesiveness and adhesiveness, compared to those of fresh albumen. Scanning electron microscopic study revealed that gel of salted albumen showed the larger voids and less compactness. In general, salting lowered trypsin inhibitory activity and gelling property of albumen from duck egg to some extent. Nevertheless, the salted albumen with the remaining inhibitor could be an alternative additive for surimi or other meat products to prevent proteolysis.

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