Food Science and Preservation (한국식품저장유통학회지)

The Korean Society of Food Preservation (한국식품저장유통학회)
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Effect of heat treatment on physicochemical properties of soybean

열처리 방법에 따른 대두의 이화학적 특성 변화

  • Kim, Sun Hee (Fermented Food Science Division, Department of Agro-food Resources, Nat'l institute of Agricultural Sciences, Rural Development Administration) ;
  • Jung, Eun Suk (Fermented Food Science Division, Department of Agro-food Resources, Nat'l institute of Agricultural Sciences, Rural Development Administration) ;
  • Kim, So Young (Fermented Food Science Division, Department of Agro-food Resources, Nat'l institute of Agricultural Sciences, Rural Development Administration) ;
  • Park, Shin Young (Fermented Food Science Division, Department of Agro-food Resources, Nat'l institute of Agricultural Sciences, Rural Development Administration) ;
  • Cho, Yong Sik (Fermented Food Science Division, Department of Agro-food Resources, Nat'l institute of Agricultural Sciences, Rural Development Administration)
  • 김순희 (농촌진흥청 국립농업과학원 농식품자원부 발효식품과) ;
  • 정은숙 (농촌진흥청 국립농업과학원 농식품자원부 발효식품과) ;
  • 김소영 (농촌진흥청 국립농업과학원 농식품자원부 발효식품과) ;
  • 박신영 (농촌진흥청 국립농업과학원 농식품자원부 발효식품과) ;
  • 조용식 (농촌진흥청 국립농업과학원 농식품자원부 발효식품과)
  • Received : 2017.09.14
  • Accepted : 2017.10.23
  • Published : 2017.10.30
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Abstract

Soybean is one of the most common food materials for making traditional Korean foods such as soybean paste, soy source and soy snack, and their manufacturing processes include heat treatment of soybean. This study was carried out to investigate the effect of heat treatment on the physicochemical properties of soybean. All samples were heat treated under commercial steamed, puffed or air-fried conditions, and then the protein molecular weight distribution, thermal properties, fluorescence intensity, protein solubility, and water and oil holding ability of the heat treated soybeans were examined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that heat treatment caused fragmentation of polypeptide chain in soybean, showing the band of low molecular ranging from 17 to 40 kDa. The differential scanning calorimetric analysis showed the decrease of enthalpy values (${\Delta}H$) by heat treatment. Fluorescence spectroscopy indicated that the heat treatment caused lipid oxidation as proved by increasing emission intensity. The protein solubility at pH 3-6, and water holding capacity of heat treated soybeans were the higher than no treatment. These results suggest that the heat treatment resulted in decreased enthalpy values, and increased protein degradation, lipid oxidation and water affinity of soybean. Moreover, the effect of heat treatment on physiochemical properties of soybeans was more significant under air-fried condition.

대두는 된장, 간장, 스낵 등 전통식품의 주요 원료이며, 열처리 공정은 대두의 가공과정에서 대부분 수반되는 단위 조작이다. 본 연구에서는 열처리가 대두의 이화학적 특성에 미치는 영향을 조사하기 위하여 상업적인 조건에서 대두를 증자, 가열팽화, 튀김 처리한 다음 단백질의 분자량 분포와 용해도, 수분과 유지 흡착력 및 열 특성과 산패도의 변화를 조사하였다. 대두는 가열처리에 의하여 단백질이 10-40 kDa 범위의 작은 분자량으로 분해되는 경향을 나타내었다. 대두의 용융 엔탈피는 199.62 J/g이었으며 열처리에 의하여 123.07-135.90 J/g 범위로 엔탈피가 감소하였고 지질 산화를 보여주는 fluorescence intensity도 열처리로 증가하였으며 열처리 효과는 튀김, 증자, 가열팽화의 순으로 높았다. 또한 대두의 수분 흡착력은 열처리 한 경우가 비열처리 대두보다 상대적으로 높았으며, 단백질의 용해도는 산성 영역(pH 3-6)에서 같은 경향을 보였다. 결과적으로 대두는 가열처리에 의하여 용융 엔탈피가 감소하고 단백질이 분해되며 지질 산화와 용해도 및 수분흡착력이 증가하는데 대두에 대한 열처리의 효과는 튀김 공정에서 뚜렷하였다.

Keywords

References

  1. Kim SO (2006) Research and industrial trend of the functional components of soybean. Food Science and Industry, 39, 2-10
  2. Giese J (1994) Proteins as ingredients: Types, functions, applications. Food Technol, 48, 50-60
  3. Kolar CW, Richert SH, Decker CD, Steinke FJ, Vander ZRJ (1985) Isolated soy protein. In: New protein foods, Altschul AM, Wilcke HL (Editor), Academic Press Inc, New York, NY, USA, p 259-299
  4. Coward L, Barnes NC, Setchell KDR, Barncs S (1993) Genistein, daidzein and their ${\beta}$-glucosidase conjugates: Antitumer isoflavones in soybean foods from Amenrican and Asia diets. J Agric Food Chem, 41, 1961-1967 https://doi.org/10.1021/jf00035a027
  5. Potter SM, Baum JA, Teng H, Stillman RJ, Shay NF, Erdman JW Jr (1998) Soy protein and isoflavones: Their effects on blood lipids and bone density in postmenopausal woman. Am J Clin Nutr, 68, 1375S-1379S https://doi.org/10.1093/ajcn/68.6.1375S
  6. Matthan NR, Jalbert SM, Ausman LM, Kuvin JT, Karas RH, Lichtenstein AH (2007) Effect of soy protein from differently processed products on cardiovascular disease risk factors and vascular endothelial function in hypercholesterolemic subjects. Am J Clin Nutr, 85, 960-966 https://doi.org/10.1093/ajcn/85.4.960
  7. Chun JK, Kim KH, Mok CK, Lee SJ, Kwon YA (2003) Food Engineering. McGraw-Hill Korea Inc, Seoul, Korea, p 283-286, 321
  8. Shu TS, Lee G, Seo YK, Lee KP, Kim DJ (2004) Micro particle technology in food science. Food Science and Industry, 37, 17-21
  9. Yang JB, Ko MS, Moon YH (2009) Physicochemical changes in pork loins affected by different cooking methods. Korean J Food preserv, 16, 534-540
  10. Kim SY, Park PSW, Rhee KC (1990) Functional properties of proteolytic enzyme modified soy protein isolate. J Agric Food Chem, 38, 651-656 https://doi.org/10.1021/jf00093a014
  11. Franzen KL, Kinsella JE (1976) Functional properties of succinylated and acetylated soy protein. J Agric Food Chem, 24, 788-795 https://doi.org/10.1021/jf60206a036
  12. Messina MJ, Persky V, Setchell KDR, Barnes S (1994) Soy intake and cancer risk: A review of the in vitro and in vivo data. Nutr Cancer, 21, 113-131 https://doi.org/10.1080/01635589409514310
  13. Kim SH, Hwang IK (1998) Physicochemical characteristics of lipoxygenase-deficient soybeans. Korean J Food Sci Technol, 30, 751-758
  14. Clarkson TB (2002) Soy, soy phytoestrogens and cardiovascular disease. J Nutr, 132, 566S-569S https://doi.org/10.1093/jn/132.3.566S
  15. Lee CH, Yang L, Xu JZ, Yeung SYV, Huang Y, Chen ZY (2005) Relative antioxidant activity of soybean isoflavones and their glycosides. Food Chem, 90, 735-741 https://doi.org/10.1016/j.foodchem.2004.04.034
  16. Son DY, Lee BR, Shon DW, Lee KS, Ahn KM, Nam SY, Lee SI (2000) Allergenicity change of soybean proteins by thermal treatment. Korean J Food Sci Technol, 32, 959-963
  17. Molina E, Defaye AB, Ledward DA (2002) Soy protein pressure-induced gels. Food Hydrocoll, 16, 625-632 https://doi.org/10.1016/S0268-005X(02)00028-0
  18. Yoon HH, Jeon EJ (2003) Characteristics of soybean soaking water after heat treatment. Korean J Food Sci Technol, 35, 1098-1103
  19. Ryu CH, Lee JO, Son DY (2012) Reduction of allergic potential of Meju by three step fermentation. J Korean Soc Food Sci Nutr, 41, 1066-1071 https://doi.org/10.3746/jkfn.2012.41.8.1066
  20. Seol HG, Ko YJ, Kim EJ, Lee GL, Kim DG, Lee JO, Ahn KM, Ryu CH (2012) Allergenicity change of soybean proteins by thermal treatment methods. J Life Sci, 22, 524-531 https://doi.org/10.5352/JLS.2012.22.4.524
  21. Yoon HH, Jeon EJ (2004) Functional properties of soy protein isolate from heat treated soybean. Korean J Food Sci Technol, 36, 38-43
  22. Cha YH (2011) Effect of ohmic heating on characteristics of heating denaturation of soybean protein. Korean J Food Nutr, 24, 740-745 https://doi.org/10.9799/ksfan.2011.24.4.740
  23. AOAC (2000) Official Methods of Analysis. 17th ed, Association of Official Analytical Communities, Washington DC, USA, Method 991.43
  24. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 https://doi.org/10.1038/227680a0
  25. Morr CV, German B, Kinsella JE, Regenstein JM, Van Buren JP, Kilara A, Lewis BA, Mangino ME (1985) A collaborative study to develop a standardized food protein solubility procedure. J Food Sci, 50, 1715-1718 https://doi.org/10.1111/j.1365-2621.1985.tb10572.x
  26. Beuchat LR (1977) Functional and electrophoretic characteristics of succinylated peanut flour protein. J Agric Food Chem, 25, 258-261 https://doi.org/10.1021/jf60210a044
  27. Tang CH, Chen Z, Li L, Yang XQ (2006) Effects of transglutaminase treatment on the thermal properties of soy protein isolates. Food Res Int, 39, 704-711 https://doi.org/10.1016/j.foodres.2006.01.012
  28. Kikugawa K (1986) Fluorescent products derived from the reaction of primary amines and components in peroxidized lipids. Adv Free Radical Biol Med, 2, 389-417 https://doi.org/10.1016/S8755-9668(86)80020-5
  29. Uhm JT, Yoon WB (2012) Development of a direct evaluation method to measure the rancidity of Yeonhaeju soybean (Bazaz) powders during storage via the fluorescence spectrum test. Korean J Food Preserv, 19, 639-644 https://doi.org/10.11002/kjfp.2012.19.5.639
  30. KIM JS, Park SJ, Choi MK, Moon EY, Kang MH (2010) Comparison of physicochemical properties between organic and conventional soybean by steaming treatment. J East Asian Soc Dietary Life, 20, 963-968
  31. Petruccelli S, Aon MC (1996) pH-induced modifications in the thermal stability of soybean protein isolates. J Agric Food Chem, 44, 3005-3009 https://doi.org/10.1021/jf9600061
  32. Han GD, Fan JP, Suzuki A (2006) Changes of SDS-PAGE pattern and allergenicity of BSA and BGG in beef extract treated with heat and high pressure. J Korean Soc Food Sci Nutr, 35, 594-599 https://doi.org/10.3746/jkfn.2006.35.5.594
  33. Wang C, Johnson LA (2001) Functional properties of hydrothemally cooked soy protein products. J Am Oil Chem Soc, 78, 189-195 https://doi.org/10.1007/s11746-001-0242-y
  34. Philips RD, Beuchat LR (1981) Enzyme modification of proteins. In: Protein Functionality in Foods, Cherry JP (editor), Am Chem Soc, Washington DC, USA, p 275
  35. Mirsky AE, Pauling L (1936) On the structure of native denatured and coagulated proteins. Proc Natl Acad Sci USA, 22, 439-447 https://doi.org/10.1073/pnas.22.7.439
  36. Kang YJ (1984) Enzymatic modification of soy proteins: Effects of functional properties of soy isolate upon proteolytic hydrolysis. Korean J Food Sci Technol, 16, 211-217
  37. Arntfield SD, Murray ED (1981) The influence of processing parameters on food protein functionality: I. Differential scanning calorimetry as an indicator of protein denaturation. Can Inst Food Sci Technol J, 14, 289-294 https://doi.org/10.1016/S0315-5463(81)72929-8
  38. Sorgentini DA, Wagner JR, Anon MC (1995) Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions. J Agric Food Chem, 43, 2471-2479 https://doi.org/10.1021/jf00057a029
  39. Renkema JMS, Knabben JHM, van Vliet T (2001) Gel formation by ${\beta}$-conglycinin and glycinin and their mixtures. Food Hydrocolloids, 15, 407-414 https://doi.org/10.1016/S0268-005X(01)00051-0
  40. Kuen S (2004) Effect of temperature and pH on the solubility of soy protein. Chemical Engineering undergraduate. Ph D Thesis, The University of Queensland, Australia, p 74
  41. Kikugawa K, Machida Y, Kida M, Kurechi T (1981) Studies on peroxidized lipids. III. Fluorescent pigments derived from the reaction of malonaldehyde and amino acids. Chem Pharm Bull, 29, 3003-3011 https://doi.org/10.1248/cpb.29.3003
  42. Kikugawa K, Ido Y (1984) Studies on peroxidized lipids. V. Formation and characterization of 1,4-dihydropyridine-3,5-dicarbaldehydes as model of fluorescent components in lipofuscin. Lipids, 19, 600-608 https://doi.org/10.1007/BF02534718
  43. Estevez M, Kylli P, Puolanne E, Kivikari R, Heinonen M (2008) Fluorescence spectroscopy as a novel approach for the assessment of myofibrillar protein oxidation in oil-in-water emulsions. Meat Sci, 80, 1290-1296 https://doi.org/10.1016/j.meatsci.2008.06.004