지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.10 No.2
- 발행연도
- 2005.6
- 수록면
- 191 - 197 (7page)
이용수
초록· 키워드
오류제보하기
There exist two interesting phenomena in making seafood products from surimi. When salted surimi is kept at a constant low temperature (4~40℃), its rheological properties change from sol to gel, which is called “setting”. Seafood processors can exploit changes that occur during setting in preparation of surimibased products, because heating at high temperatures, after the pre-heating during the setting process, enhances the gel-strength of salted surimi. Contrarily, when salted surimi or low-temperature set gel is heated at moderate temperatures (50~70℃), a deterioration of gel is observed. The phenomenon is termed “modori”. In the modori temperature range, heat-stable cysteine proteinases such as cathepsin B, H, L and L-like hydrolyze the myosins responsible for gel-formation, resulting in gel weakening modori. This article reviews molecular events occurring during gel setting that improve the quality of surimi-based products, and inhibition of modori by applying proteinase inhibitors. Application of recombinant protein technology to surimi-based products is introduced and its prospects for practical use are discussed.
목차
Abstract
INTRODUCTION
STRUCTURAL CHARACTERISTICS OF FISH MYOSIN
LOW - TEMPERATURE GELATION “SETTING” OF SURIMI
MODERN SURIMI TECHNOLOGIES TO PREPARE HIGH QUALITY SURIMI - BASED PRODUCTS
PRODUCTION AND APPLICATION OF GENETICALLY PRODUCED CYSTATIN C, A CYSTEINE PROTEINASE INHIBITOR
CONCLUSION
REFERENCES
참고문헌 (64)
참고문헌 신청
An H, Peters MY, Seymour TA. 1996. Roles of endogeneous enzymes in surimi gelation. Trends Food Sci Technol 7: 321-326.
Samejima K, Ishioroshi M, Yasui T. 1981. Relative role of the head and tail portions of the molecule in heatinduced gelatin of myosin. J Food Sci 46: 1412-1418.
Watabe S, Hirayama Y, Nakaya M, Kakinuma M, Guo X-F, Kanoh S, Chaen S, Ooi T. 1998. Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature. J Them Biol 22
Ojima T, Kawashima N, Inoue A, Amauchi A, Togashi M, Watabe S, Nishita K. 1998. Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning. Fish Sci 64: 812-819.
Kawabata R, Kanzawa N, Ogawa M, Tsuchiya T. 2000. Determination of primary structure of amberjack myosin heavy chain and its relationship with structural stability of various fish myosin rods. Fish Physiol Biochem 23: 283-294.
Samejima K, Ishioroshi M, Yasui T. 1981. Relative role of the head and tail portions of the molecule in heatinduced gelatin of myosin. J Food Sci 46: 1412-1418.
Watabe S, Hirayama Y, Nakaya M, Kakinuma M, Guo X-F, Kanoh S, Chaen S, Ooi T. 1998. Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature. J Them Biol 22
Ojima T, Kawashima N, Inoue A, Amauchi A, Togashi M, Watabe S, Nishita K. 1998. Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning. Fish Sci 64: 812-819.
Kawabata R, Kanzawa N, Ogawa M, Tsuchiya T. 2000. Determination of primary structure of amberjack myosin heavy chain and its relationship with structural stability of various fish myosin rods. Fish Physiol Biochem 23: 283-294.
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