최소 단어 이상 선택하여야 합니다.
최대 10 단어까지만 선택 가능합니다.
다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기한국수산과학회지 = Korean journal of fisheries and aquatic sciences, v.54 no.4, 2021년, pp.543 - 551
임영선 (강릉원주대학교 식품영양학과) , 유병진 (강릉원주대학교 식품영양학과)
Changes in gluten surface hydrophobicity, which play an important role in the functional characteristics of protein, were measured according to various protein concentrations, pH levels, electrolytes concentrations, and alginate molecular weights using 8-anilino-1-naphthalene sulfonic acid (ANS) as ...
Bonomi F, Mora G, Pagani MA and Iametti S. 2004. Probing structural features of water-insoluble proteins by front-face fluorescence. Anal Biochem 329, 104-111. https://doi.org/10.1016/j.ab.2004.02.016.
Chan MYY, Bell DJ and Dunnill P. 1982. The relationship between the zeta potential and the size of soya protein acid precipitate particle. Biotechnol Bioeng 24, 1897-1900. https://doi.org/10.1002/bit.260240817.
Damodaran S. 1996. Amino acids, peptides and proteins. In: Food chemistry. Fennema OR ed. Marcel Dekker, New York, NY, U.S.A., 321-429.
Dickinson E and Stainsby G. 1988. Emulsion stability. In: Advances in food emulaions and foams. Elsevier, Cambridge, MA, U.S.A., 1-44.
Domenek S, Morel MH, Redi A and Guilbert S. 2003. Rheological investigation of swollen gluten polymer networks, effects of process parameters on cross-link density. Macromol Symp 200, 137-146. https://doi.org/10.1002/masy.200351014.
Drohan DD, Tziboula A, McNulty D and Horne DS. 1977. Milk protein-carrageenan interactions. Food Hydrocoll 11, 101-107. https://doi.org/10.1016/S0268-005X(97)80016-1.
Fioramonti SA, Perez AA, Aringoli EE and Rubiolo AC. 2014. Design and characterization of soluble biopolymer complexes produced by electrostatic self-assembly of a whey protein isolate and sodium alginate. Food Hydrocoll 35, 129-136. https://doi.org/10.1016/j.foodhyd.2013.05.001.
Frederick FS. 1994. Interaction of soy isolate with polysaccharide and its effect on film properties. J Am Oil Chem Soc 71, 1281-1285. https://doi.org/10.1007/BF02540552.
Galazka VA, Smith D, Ledward DA and Dickinson E. 1999. Complexes of bovine serum albumin with sulphated polysaccharides: effects of pH, ionic strength and high pressure treatment. Food Chem 64, 303-310. https://doi.org/10.1016/S0308-8146(98)00104-6.
Gennadios A, Brandenburg AH, Weller CL and Testin RF. 1993. Effect of pH on properties of wheat gluten and soy protein isolate films. J Agric Food Chem 41, 1835-1839. https://doi.org/10.1021/jf00035a006.
Gianibelli MC, Larroque OR, MacRitchie F and Wrigley CW. 2001. Biochemical, genetic and molecular characterization of wheat glutenin and its component subunits. Cereal Chem 78, 635-646. https://doi.org/10.1094/CCHEM.2001.78.6.635.
Goddard ED. 1986. Polymer-surfactant interaction. Part II. Polymer and surfactant of opposite charge. Colloids Surf 19, 301-329. https://doi.org/10.1016/0166-6622(86)80341-9.
Han C, Ma M, Li M and Sun Q. 2020. Further interpretation of th underlying causes of the strengthening effect of alkali on gluten and noodle quality: Studies on gluten, gliadin, and glutenin. Food Hydro 103, 1-11. http://doi.org/10.1016/j.foodhyd.2020.105661.
Harwalker VR and Ma CY. 1989. Effects of medium composition, preheating, and chemical modification upon thermal behavior of oat globulin and β-lactoglobulin. In: Food proteins. Kinsella JF and Soucie WG, eds. The American Oil Soc., Champaign, IL, U.S.A., 210-251.
Hayakawa S and Nakai S. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J Food Sci 50, 486-485. https://doi.org/10.1111/j.1365-2621.1985.tb13433.x.
Kato A and Nakai S. 1980. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta 624, 13-20.
Koning MMG and Visser H. 1992. Protein interactions. An overview. In: Protein interaction. Visser H. ed. VCH Publishers, New York, NY, U.S.A., 1-24.
Kundu B and Guptasarma P. 2002. Use of a hydrophobic dye to indirectly probe the structural organization and conformational plasticity of molecules in amorphous aggregates of carbonic anhydrase. Biochem Biophys Res Com 293, 572-577.
Li-Chen E, Nakai S and Wood DF. 1984. Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties. J Food Sci 49, 345-350. https://doi.org/10.1111/j.1365-2621.1984.tb12418.x.
Lim YS and Yoo BJ. 2018. Effects of average molecular weights, their concentrations, Ca ++ and Mg ++ on hydrophobicity of solution of Na-alginates prepared from sea tangle Saccharina japonicus produced in east coast of Korea. Korean J Fish Sci 51, 542-548. https://doi.org/10.5657/KFA.2018.0542.
Liu J, Luo D, Li X, L, Xu B, Zhang X and Liu J. 2016. Effects of inulin on the structure and emulsifying properties of protein components in dough. Food Chem 210, 235-241. https://doi.org/10.1016/j.foodchem.2016.04.001.
Morris C and Morris GA. 2012. The effect of inulin and fructooligosaccharide supplement on the texture, rheological and sensory properties of bread and their role in weight management. A review. Food Chem 133, 237-248. http://doi.org/10.1016/j.foodchem.2012.01.027.
Nakai S. 1983. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J Agric Food Chem 31, 676-683. https://doi.org/10.1021/jf00118a001.
Pearce KN and Kinsella JE. 1978. Emulsifying properties of protein: evaluation of turbidimetric technique. Agric Food Chem 26, 716-723. https://doi.org/10.1021/jf60217a041.
Pressini D and Sesidoni A. 2009. Effect of soluble dietary fiber addition on rheological and breadmaking properties of wheat doughs. J Cereal Sci 49, 190-201. http://doi.org/10.1016/j.jcs.2008.09.007.
Ren B, Gao Y, Lu L, Liu X and Tong Z. 2006. Aggregates of alginates binding with surfactants of single and twin alkyl chains in aqueous solutions: Fluorescence and dynamic light scattering studies. Carbohydr Polym 66, 266-273. https://doi.org/10.1016/j.carbpol.2006.03.012.
Tang Y, Yang Y, Wang Q, Tang Y, Li F and Zhao J. 2019. Combined effect of carboxymethylcellulose and salt on structural properties of wheat gluten proteins. Food Hydro 97. http://doi.org/10.1016/j.foodhyd.2019.105189.
Thomas WR. 1992. Carrageenan. In: Thickening and gelling agents for food. Imeson A ed. Blackie Academic and Professional, Cambridge, MA, U.S.A., 24-39.
Uruakpa FO and Arntfield SD. 2006. Surface hydrophobicity of commercial canola proteins mixed with κ-carrageenan or guar gum. Food Chem 95, 255-263. https://doi.org/10.1016/j.foodchem.2005.01.030.
Wang Y, Gan J, Zhou Y, Cheng Y and Nirasawa S. 2017. Improving solubility and emulsifying property of wheat gluten by deamination with four different acids: Effect of replacement of folded conformation by extended structure. Food Hydro 72, 105-114. https://doi.org/10.1016/j.food-hyd.2017.04.013.
Winnick FM. 1993. Photophysics of preassociated pyrenes in aqueous polymer solutions and in other organized media. Chemical Rev 93, 587-614. https://doi.org/10.1021/CR00018A001.
Wolf WJ. 1970. Soybean proteins: Their functional, chemical, and physical properties. J Agric Food Chem 18, 969-976. https://doi.org/10.1021/jf60172a025.
Wrigley C.1996. Giant proteins with flour power. Nature 381, 738-739. https://doi.org/10.1038/381738a0.
You BJ, Lim YS, Jeong IH and Lee KH. 1997. Effect of extraction conditions on bile acids binding capacity in vitro of alginate extracted from seatangle (Laminaria spp.). Korean J Fish Aquatic Sci 30, 31-38.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
오픈액세스 학술지에 출판된 논문
※ AI-Helper는 부적절한 답변을 할 수 있습니다.