Distribution of β-amylase and lipoxygenase in soy protein products obtained during tofu production
Article Sidebar
Main Article Content
Abstract
Soybean is considered an important source of human food and animal feed. Okara and tofu whey are the main by-products of soymilk and tofu production. The distribution of enzymes b-amylase and lipoxygenase (Lox) from six soybean genotypes in protein extracts of okara and tofu as well as in soymilk and tofu whey was assessed. SDS-electrophoretic results showed that production process significantly affected high molecular mass protein fractions of soybean by-products. Low amounts of Lox in soymilk were registered, while in okara protein extracts and tofu whey this enzyme was present in trace. In tofu protein extracts, Lox was registered in higher quantity that might be the result of the aggregation process during formation of the tofu gel. Content of b-amylase in all soy protein products was high and similar to the content in soybean genotype. Content of b-amylase in okara depended on respective soybean genotype.
Article Details
Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
Authors grant to the Publisher the following rights to the manuscript, including any supplemental material, and any parts, extracts or elements thereof:
- the right to reproduce and distribute the Manuscript in printed form, including print-on-demand;
- the right to produce prepublications, reprints, and special editions of the Manuscript;
- the right to translate the Manuscript into other languages;
- the right to reproduce the Manuscript using photomechanical or similar means including, but not limited to photocopy, and the right to distribute these reproductions;
- the right to reproduce and distribute the Manuscript electronically or optically on any and all data carriers or storage media – especially in machine readable/digitalized form on data carriers such as hard drive, CD-Rom, DVD, Blu-ray Disc (BD), Mini-Disk, data tape – and the right to reproduce and distribute the Article via these data carriers;
- the right to store the Manuscript in databases, including online databases, and the right of transmission of the Manuscript in all technical systems and modes;
- the right to make the Manuscript available to the public or to closed user groups on individual demand, for use on monitors or other readers (including e-books), and in printable form for the user, either via the internet, other online services, or via internal or external networks.
How to Cite
References
C. Fujino, S. Wada, T. Konoike, K. Toyota, Y. Suga, J. Ikeda, Effect of different organic amendments on the resistance and resilience of the organic matter decomposing ability of soil and the role of aggregated soil structure, Soil. Sci. Plant Nutr. 54 (2008) 534–542.
A.M. Jàndula, N.V. Àlvarez, M.L. Genta, Development of nutritional products with high energy and protein con-tent with raw materials from northwest region of Argentina (NOA), Univ. Nat. Tucum Inf. 15 (1991) 5–6.
A.K. Smith, J.S. Circle, Chemical composition of the seed, In: K.A. Smith, S.J. Circle (Eds.), Soybeans: chemistry and technology, AVI Pub. Co. INC, Westport, CN, 1972, pp. 61–92.
S.P. Stanojevic, M.B. Barac, M.B. Pesic, B.V. Vucelic-Radovic, Assessment of soy genotype and processing method on quality of soybean tofu, J. Agric. Food Chem. 59 (2011) 7368–7376.
P. Siddhuraju, K. Becker, P.S. Harinder, S.P.H. Makkar, Studies on the nutritional composition and antinut-ritional factors of three different germplasm seed materials of an under-utilized tropical legume, Mucuna pruriens Var. Utilis, J. Agric. Food Chem. 48 (2000) 6048–6060.
D.K. OToole, Characteristics and use of okara, the soy-bean residue from soy milk production – A review, J. Agric. Food Chem. 47 (1999) 363–371.
S.P. Stanojevic, M.B. Barac, M.B. Pesic, V.B. Vucelic-Radovic, Composition of proteins in okara as a byproduct in hydrothermal processing of soymilk, J. Agric. Food Chem. 60 (2012) 922–9228.
C. Wang, L.A. Johnson, L.A. Wilson, Calcium coagulation properties of hydrothermally processed soymilk. J. Am. Oil Chem. Soc. 80 (2003) 1225–1229.
S.P. Stanojevic, Biochemical properties of proteins and carbohydrates of modified soy protein products, Doctoral Thesis, Faculty of Agriculture, University of Belgrade, 2007.
M. Friedman, Nutritional value of proteins from different food sources – A Review, J. Agric. Food Chem. 44 (1996) 6–29.
M. Friedman, D.L. Brandon, Nutritional and health benefits of soy proteins, J. Agric. Food Chem. 49 (2001) 1069–1086.
D. Devine, Soya and health 2002 – clinical evidence, dietetic applications, British Nutrition Foundation, Nutrit. Bull. 27 (2002) 195–198.
M. Barać, S. Stanojević, M. Pesic, Biologically active components of soy bean - A rewiev, Acta Periodica Technol. 36 (2005) 155–169.
I. Meteos-Aparicio, A.C. Redondo, M.J. Villanueva-Suárez, A M. Zapata-Revilla, Soybean, a promising healt source, Nutr. Hosp. 23 (2008) 305–312.
FAO/WHO Expert Committee on food additives, Sum-mary and conclusions, In Proceedings of 53rd Meeating, Roma, June, 1990, pp. 1–10.
E. Mori, B. Mikami, Y. Morita, B. Jirgensons, Circular dichroism and the conformational properties of soybean β-amylase, Arch. Biochem. Biophys. 211 (1981) 382–389.
N.Y. Kang, A. Tanabe, M. Adachi, S. Utsumi, B. Mikami, Structural analysis of threonine 342 mutants of soybean β-amylase: Role of a conformational change of the inner loop in the catalytic mechanism, Biochemistry 44 (2005) 5106–5116.
J. Fukumoto, Y. Tsujisaka, Kagaku to Kogyo, Osaka, Sci. Ind. 28 (1954) 282–287.
Y. Moriota, F. Yagi, S. Aibara, Chemical composition and properties of soybean β-amylase, Biochemistry 79 (1976) 591–603.
B. Mikami, M. Degano, E.J. Hehre, C.J. Sacchettini, Crystal structures of soybean β-amylase reacted with
β-maltose and maltal: Active site components and their apparent roles in catalysis, Biochemistry 33 (1994) 7779–7787.
E. Sarikaya, T. Higasa, M. Adachi, B. Mikami, Comparison of degradation abilities of α- and β-amylases on raw starch granules, Process Biochem. 35 (2000) 711–715.
H. Ren, F.J. Thompson, J.T. Madison, Biochemical and physiological studies of soybean β-amylase, Phyto-chemistry 33 (1993) 541–545.
M. Adachi, B. Mikami, T. Katsube, S. Utsumi, Crystal structure of recombinant soybean β-amylase complexed with β-cyclodextrin, J. Biol. Chem. 273 (1998) 19859–19865.
B. Mikami, K. Nomura, Y. Morita, Two sulfhydril groups near the active site of soybean β-amylase, Biosci. Biotech. Biochem. 58 (1994) 126–132.
A. Hirata, M. Adachi, A. Sekine, Y.N. Kang, S. Utsumi, B. Mikami, Structural and enzymatic analysis of soybean
β-amylase mutants with increased pH optimum, J. Biol. Chem. 279 (2004) 7287–7295.
A. Gertler, Y. Birk, The role of sulphydryl groups in soybean β-amylase, Biochim. Biophys. Acta 11 (1996) 898–105.
F. Franks, Introduction. In: Characterization of proteins, Franks F., Eds.; Publisher: Cambridge, UK: Pafra, Ltd., (1988) 1–8.
C. Fukazawa, Method for separation of beta-amylase, Patent number 05294341, Tsukuba, 1994.
M. Miwa, L.Z. Kong, K. Shinohara, M. Watanabe, Soy-bean trypsin inhibitor and β-amylase stimulate macro-phages, Biochem. Biophys. Res. Commun. 173 (1990) 296–301.
S. Iwabuchi, F. Yamauchi, Electrophoretic analysis of whey proteins present in soybean globulin fractions, J. Agric. Food Chem. 35 (1987) 205–209.
H. Hirano, H. Kagawa, Y. Kamata, F. Yamauchi, Structural homology among the major 7S globulin subunits of soybean seed storage proteins, Phytochemistry 26 (1987) 41–45.
J.J. Rackis, D.J. Sessa, H.D. Honig, Flavor problems of vegetable food proteins, J. Amer. Oil Chem. Soc. 56 (1979) 262–271.
S.P. Stanojevic, M.B. Barac, M.B. Pesic, V.S. Jankovic, B.V. Vucelic-Radovic, Bioactive proteins and energy value of okara as a byproduct in hydrothermal pro-cessing of soy milk, J. Agric. Food Chem. 61 (2013) 9210–9219.
S.P. Stanojevic, M.B. Barac, M.B. Pesic, S.M. Zilic, M.M. Kresovic, B.V. Vucelic-Radovic, Mineral elements, lipoxygenase activity and antioxidant capacity of okara as a byproduct in hydrothermal processing of soy milk, J. Agric. Food Chem. 62 (2014) 9017–9023.
W.W. Christe, Extraction of lipids from samples, Lipid Technol. 5 (1993) 18-19.
P.S. Fling, S.D. Gregerson, Peptide and protein mole-cular weight determination by electrophoresis using a high-molarity Tris-buffer system without urea, Anal. Biochem. 155 (1986) 83–88.
S.M. Žilić, M.B. Barać, M.B. Pešić, S.D. Mladenović-Drinić, D.D. Ignjatović-Micić, M. Srebrić, Characterization of proteins from kernel of different soybean varieties, J. Sci. Food Agric. 91 (2010) 60–67.
C.L. Ren, M. Tang Zhang, S. Guo, Interactions between whey soybean protein (WSP) and β-conglycinin (7S) during the formation of protein particles at elevated temperatures, Food Hydrocolloid. 23 (2009) 936–941.
P. Lopez, J. Burgos, Lipoxygenase inactivation by mano-thermosonication: effects of sonication physical para-meters, pH, KCl, sugars, glycerol, and enzyme concentration, J. Agric. Food Chem. 43 (1995) 620−625.
N. Yoshigi, Y. Okada, H. Maeba, H. Sahara, T. Tamaki, Role of the C-terminal region of β-amylase from barley and additivity of mutational effects of intragenic amino acid replacements on the thermostability of β-amylase, J. Appl. Glycosci. 43 (1996) 227–235.