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Overview of Soybean Processing and Products

Compositional Changes in Trypsin Inhibitors, Phytic Acid, Saponins and Isoflavones Related to Soybean Processing12
Agricultural Research Biopolymer Research, National Center for Agricultural Utilization Research, Service, U.S. Department of Agriculture, PeorÃ-a,IL 61604

ABSTRACT Soybeans are high in protein but also contain a number of minor constituents traditionally considered to be antinutritional factors. These include trypsin inhibitors, phytic acid, saponins and ¡soflavones. These compounds are now thought to have beneficial biological effects in the diet, such as lowering blood cholesterol or preventing cancer. Soybean processing changes the content of these minor constituents in var ious ways. This review discusses the changes in content of trypsin inhibitors, phytic acid, saponins and ¡sofla vones as soybeans are processed into the conventional protein ingredients, flours, concentrates and isolates, as well as some of the traditional Oriental soybean foods. J. Nutr. 125: 581S-588S, 1995.

The proteins of soy contribute to the nutritional value of foods and feeds and are responsible for a number of functional characteristics in a variety of foods. Heating is necessary to attain maximum nutri tional value and to modify functional properties of soybean protein. Kakade et al. (1973), using immobilized trypsin to remove trypsin inhibitors from a raw soy flour extract followed by rat feeding experiments, concluded that approximately 40% of the growth-depressing effect of the unheated extract was due to the trypsin inhibitors. The remainder of the growth depression was attributed to poor digestibility of the undenatured protein.

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• soybean • isoflavone • phytic acid • saponin • trypsin inhibitor

Trypsin inhibitors
Although soybean protein products require heat processing to achieve maximum nutritional value, partly through trypsin inhibitor denaturation, trypsin inhibitors also display anticarcinogenic properties (Messina and Barnes 1991). The predominant trypsin inhibitors in soybeans and derived materials are pro teins and they are located, for the most part, with the main storage proteins in the protein bodies of the cotyledon (Horisberger et al. 1986, Horisberger and Tacchini-Vonlanthen 1983a, Horisberger and Tacchini-Vonlanthen 1983b). This being the case, trypsin inhibitors tend to fractionate with the milieu of stor age proteins as soybeans are processed into ingredients and foods. There are exceptions to this generality that
1Presented at the First International Symposium on the Role of Soy in Preventing and Treating Chronic Disease, held in Mesa, AZ, February 20-23, 1994. The symposium was sponsored by Protein Technologies International, the soybean growers from Nebraska, Indiana and Iowa and the United Soybean Board. Guest editors for this symposium were Mark Messina, 1543 Lincoln Street, Port Townsend, WA 98368, and John W. Erdman, Jr., Division of Nu tritional Sciences, University of Illinois, Urbana, IL 61801-3852. 2The mention of firm names or trade products does not imply that they are endorsed or recommended by the U.S. Department of Agriculture over other firms or similar products not mentioned.

Processing of soybeans, whether by traditional or Western methods, is necessary to produce animal feed ingredients, food for human consumption or func tional protein ingredients intended for incorporation into a wide variety of human foods. During the course of soybean processing to change properties, the chem ical composition may change as well. In this review we summarize the compositional changes that occur in trypsin inhibitors, phytate, saponins and isoflavones as a result of processing. Proteins The content and properties of oil and protein are the primary determinants of whole soybean value. Oil and protein are separated from each other early in most Western processing; in some traditional Oriental soy foods, oil and protein remain together whereas in oth ers they are separated. Soybean oil is not included in this discussion.
0022-3166/95 $3.00 © 1995 American Institute of Nutrition.


Try psi a inhibitor con ten t of soybeans and processed soy Oriental and other soybean foods are generally low protein products in trypsin inhibitor (Table 2).2-30.49. has a trypsin inhibitor 6 Peace et by on December 30.9 trypsin units.322.73.1 to 19.4-7. Miso is a product made by fer flour5Concentrate6Isolate5'616.2-1. content (9 mg/g of protein. after analyzing 108 strains and culphoresis and the Bowman-Birk inhibitor was measured tivars. Heated or toasted flours are produced having a range of trypsin inhibitor activities depending upon their intended use. In these processes oligosaccharides Type and other constituents are removed but most of the mg/g sample mg/g protein protein is not. 21'3 Whole soybeans the protein inhibitors but the origin of the measured flour5Toasted Raw 28-327. sin inhibitor levels in the range of 1-30 mg/g or. The ranges of trypsin inhibitor ac Soy sauce2Miso tivity are given in Table 1.7-122. Table 2) near to that as sociated with a fully toasted soy flour (16 mg/g of pro tein. (1985).1—0. contents ranged from <0. Soy protein isolates are processed to contain >90% infant formula30. Rackis et al. Table 1).4 activity is uncertain. none of the trypsin inhibitors are re 6. reviewed the literature through 1985 on protease in The trypsin inhibitor level in these products falls in the range of 0. which is made from heated soybean milk by of pure trypsin has an activity of 1.6 mg/g and from <0. (1986) protein isolate with the addition of other nutrients. Based on 19 varieties and strains. 'Doelletal. (1972). are subject to Birk inhibitors.3 mg/g of protein equivalent.34. miso by extraction. originally expressed as trypsin units inhibited. a process in which the hulls and tively. It mg/g sample mg/g protein is unlikely that these values represent activity from 63'4 7-27.60. coagulation of the proteins with a salt such as calcium 5 Rackis et al. were miso is heated. Soy sauce. (1981). The Kunitz soybean trypsin inhibitor the main species. 57. (1992).0 mg/g.3-2.3 to 2. isolates contain tryp 3 Peace et al.1 mg/g of Kunitz and <0. 4 Kakade et al.5 protein. 2009 . When soybeans are processed into mg/g of Kunitz and Bowman-Birk inhibitors.9 hibitor/g of protein.3 mg/g of sample or 3. (1972). 5-7 mg trypsin inhibitor/ (unextracted)2Miso (defatted)2Tofu2Soy g of concentrate or 8-11 mg/g of concentrate protein. sulfate followed by cooling. for Kunitz and BowmanTrypsin inhibitors.3-3 mg/g of sample or 2-16 mg/g of hibitor content of some plant foods. whole soybeans protein (Table 2). is low in trypsin inhibitor content at 0. reported they contain 35-123 mg trypsin inby chymotrypsin inhibition.94.5oil are removed.31.034.6 mg/g and from 0. Soy protein concentrates are produced Trypsin inhibitor content of Oriental and other soy foods by washing defatted flours with either aqueous ethanol Trypsin inhibitor activity1 or acidified water. Table 2 shows a value of 4 mg/g of sample or 23 mg/g of pro tein for miso.2-15.21. be Downloaded from jn.22. converted to trypsin inhibitor units with the relationship that l pg Tofu. when lipids are removed from 1Measured by trypsin inhibition. the same range per gram of protein (Table 1). Soybeans are approximately 40% protein and Ka kade et al. which equates to approxi Birk inhibitors whereas soy protein isolate inhibitor mately 58 mg trypsin inhibitor/g of protein (Table 1). the trypsin inhibitor level falls to 1 Hafez (1983). respectively. A dehydrated soymilk was found to denaturation and inactivation by heat.9-9. Soy flours were found to contain from 1.0 mg/g of Bowmanmoved but they become enriched in the flour to levels of 28-32 mg/g of flour. Depending upon the amount of washing of the precipitated curd as well as the trypsin inhibitor 1Measured by trypsin inhibition. (1992). respec raw defatted flour. Soy infant formula is made from soy will be discussed as they arise.nutrition. 4 mg/g of protein and it will decrease further if the 3 Values.582S TABLE 1 SUPPLEMENT cause nearly all of this product is protein. the Kunitz trypsin inhibitor (Table present was quantitated by rocket immunoelectro1). A fully toasted soy flour will have a trypsin inhibitor level of only 8-9 mg/g of flour or approximately 16 TABLE 2 mg/g of protein.815. Concentrate samples contained a range of <0. the protein content is therefore in creased to >65%. were reported to contain 17-27 mg of trypsin inhibDiPietro and Liener (1989) differentiated between the Kunitz and Bowman-Birk inhibitor content of itor/g (Hafez 1983) according to activity assays with the results expressed as though all activity resided in soybean flours. produced by enzymic or acidic hydrolysis of a mixture of soybeans Trypsin inhibitor activity1 Type and wheat. However. mentation of soaked and steamed soybeans.4-29.5 to 3.4-11.98. content of the starting soybeans. concentrates. being proteins.2 to 4. isolates and a variety of foods (Table 3).

811.730. consequently.9 mg/g Bowman-Birk inhibitor whereas a wheat-soy pancake mix had 1. phytic acid is stable to cooking (Davies and Reid 1979) and probably is not degraded during texturization by extrusion. fall into the range of 1. (1989)Sutardi (1985)Thompson and Buckle Erdman(1982)Beleiaet and (1993)Ranhotraet al.500.2-4.1-0. Phytic acid Phytic acid has long been recognized to interfere with the absorption of minerals.1-19.4 mg/g of BowmanBirk inhibitors. et al.5-6. (1974)Schuster et al. Table 4 also lists the various fractions and protein products that are derived from soybeans.39-2.51-1.8% phytic acid. which contain only 0.5-1. Full-fat flour. (1980) matter1.69-0. Values for defatted flours. there is renewed interest in this compound. The lower values for tempeh are attributed to partial hydrolysis by phytase elaborated by Rhizopus oligosporus.5-2. However. concentrates or isolates.120. which is essentially the cotyledon fraction.0 mg/g of Kunitz and 0.0<0.300. Texturized flours and concentrates are also in this range. Field type cultivars. especially zinc. The phytic acid values fall in the range of 1-3% except for okara and tempeh.581. 4 Fifteen samples. A variety of other soy containing foods were found to have no more than approximately 1% of the quantity of these inhibitors present in raw soy flours.3%. contain which is localized in the protein bodies and ap pears to be distributed between soluble protein-phytate salts and insoluble globoid inclusions (Prattley and Stanley 1982). (1980)Davies Bodwell and (1979)Harland and Reid Oberleas(1977)Ranhotra and (1974)Harlandal.880.1.4 1 Kunitz inhibitor measured by rocket immunoelectrophoresis.31. et Oberleas(1977)Schuster and (1980)Honig Bodwell and (1984)O'Neill et al.01.9<0. Bowman-Birk inhibitor measured by chymotrypsin inhibition.00-1. The hulls contain only 0.96Omosaiye (1985)Sudarmadji and Buckle Markakis(1977) and .org by on December 30.6% phytic acid.611.2-1.471.831.6<0.51.2% phytic acid. Phytic acid content of soybeans can vary considerably (Table 4). soymilkWheat-soy pancake mix1.881.5 and 8.5% phytic acid whereas the hypocotyl contains 0.0-2.3-2. der Riet soymilk)TempehTempeh1. (1989)Schaeferet al. concentrates and isolates likewise are in the range of 1-2% phytic acid despite considerable additional processing as compared with full-fat flours. (1974)Ranhotra al. (1984|Lehrfeld et al.62-1.nutrition. Data on Oriental soybean foods are given in Table 5. 2 Thirty-eight field-type varieties. 3 Authors did not specify whether products were derived from flours.COMPOSITIONAL CHANGES WITH SOYBEAN PROCESSING TABLE 4 583S TABLE 3 Kunitz and Bowntaa-Birk soy protein products trypsin inhibitors and some foods1 Kunitz inhibitor in Phytic acid content of soybeans and processed soy protein products acid ProductSoybeans'Soybeans2HullsHullsHypocotylCotyledonsFull-fat contentg/100gdry Sample Bowman-Birk inhibitor mg/g sample FloursConcentratesIsolatesDehydrated (1976)Raboy et al. thus the bulk of the phytic acid occurs in the cotyledons.5-1. Data from DiPietro and Liener (1989). flourDefatted flourDefatted flourTextured flourTextured vegetableprotein3ConcentrateTextured Downloaded from jn. the hulls (8%) plus the hypocotyl (2%) represent only approximately 10% of the seed.5-3. 2009 concentrateIsolate4IsolateSpun isolate fiberPhytic 1 Fifteen field-type varieties. the organism used in fer- TABLE S Phytic acid content of OrÃ-en soy foods tal Product Phytic acid content g/JOO g dry matter Reference SoymilkSoymilkTofuTofuOkara Cheryan(1979)Beleiaet and (1990)van al. Re cent work suggests that phytic acid may have anticarcinogenic properties as well (Messina and Barnes 1991). The ratio of Kunitz inhibitor to Bowman-Birk inhibitor ranged between 0. contains 1.96-2. der Riet (1992)van and Love (residuefrom (1989)Sutardi et al. The cotyledons contain 1.20. which are the usual items of commerce.681.1<0.3 mg Kunitz inhibitor/g and 1.9%.

4 Taniyama et al. rats and mice failed to inhibit growth even when fed at levels three to five times those of a normal soybean meal diet (Ishaaya et al. 2 Ireland et al.47 0. by on December 30. . However.09-0. Unheated and heated full-fat flours contain approxi mately 0. Okara (the insoluble residue remaining after preparation of soymilk). Saponins Most listings of soybean antinutritional factors in the past included saponins. More recently.5% saponins.98 0 0. Other soyasapogenols reported earlier evidently were artifacts of hydro lysis conditions (Price et al. 1993) as well as the aglycones obtained upon acid hydrolysis of the saponins (Ireland et al. seed parts and derived protein products.1-0.67-1.3-dihydro-2. 1987). Fenwick and Oakenfull 1983) gave values that were almost 10-fold too high. The seed coat (hull) contains no saponins.5-dihydroxy-6-methyl-4Hpyran-4-one attached to the C-22 hydroxyl group of soyasapogenol B. The cotyledons contain 0.22-0. Attention is also called to the fact that some of the early results obtained by thin layer chromatography (Fenwick and Oakenfull 1981. tofu and natto is in the range of 0. it has little effect on the composition of flours and related products that may contain this fraction. Kitagawa et al. results in some degradation of the saponins and thus a lower saponin content as compared with soybeans.53 0. 1993). This diversity of structure and composition has also made it difficult to analyze for soybean saponins. soyasapogenol A. there is justification for removing saponins from the list of antinutritional factors in soybeans (Liener 1981).33 0. Soybean saponins are complex compounds consist ing of nonpolar triterpenoid alcohol aglycones linked to one or more polar oligosaccharides resulting in molecules with amphiphilic properties similar to de tergents. the results indicate that the sa ponins are heat stable (except for such changes as re ported by Kudou et al.4%.1-0. unheated2 Full-fat flour. Five major saponins have been isolated and structurally characterized (Kitagawa et al.3% saponins whereas the level in the hypocotyl approaches 2%. results may not always agree with analysis of intact saponins. hypocholesterolemic and anticarcinogenic effects have been attributed to soybean saponins (Messina and Barnes 1991). the saponins tend to remain with the protein products derived from soybeans. (1984). 0. most reviewers have ignored studies reported 25 years ago showing that feeding soybean saponins to chicks. the saponins apparently complex with the proteins and hence are retained with the proteins during the isolation process.nutrition.21-0. 1985).2-0. However. (1988). the high end of the range depends on a value determined by analysis of the sapogenols. yuba. in deed. Addi tional complexity has been reported recently in the form of 2. heated2 Protein concentrate2 Protein isolate2 1 Kitagawa et al. although with little or no justification. Although water soluble. 3 Shiraiwa et al. 1969). hence. Saponin content of several Oriental foods (Table 7) such as soymilk. Soybeans contain 0. Isolates have been reported to contain 0. 1986).584S SUPPLEMENT menting cooked soybeans to produce tempeh (Sudarmadji and Markakis 1977.8% saponins. this group is removed with the for mation of maltol when the saponins are heated (Kudou et al. occur in intact saponins. Table 6 shows saponin contents for soybeans. Fermentation. Consequently. Sutardi and Buckle 1985). as in the preparation of miso. 1988b). (1991). 1993). No saponins were de tected in a protein concentrate prepared by aqueous alcohol extraction as would be expected based on the solubility properties of the saponins. Early studies resulted in confusion about the number and structures of the aglycones but it is now believed that only three aglycones. miso (fermented soybean paste) and natto (fermented.27 1.3-0. 2009 and problems of analysis are reviewed by Price et al. Structural studies TABLE 6 Saponin content of soybeans and processed soy protein products Product Saponin content g/100g dry matter Soybeans' Soybeans2 Soybeans3 Cotyledons4 Hypocotyl-radicle4 Seed coat (hulls]4 Full-fat flour.3%. which may be free or acetylated (Kitagawa et al. The latter method assumes that the ratio of aglycone to sugars is 1:1 and this is not always justified (Price et al. 1985b.81 Downloaded from jn. With the exception of alcohol-extracted concen trates. the hypocotyl represents only approximately 2% of the seed. These high values apparently resulted from impurities and use of a nonspecific de tection reagent (Curl et al.32 0. (1986|. hence. cooked soybeans) tend to be somewhat lower in saponin content at 0.5% saponins. 1988a). 1986). Kitagawa et al. B and E. A variety of methods have been reported but at present high performance liquid chromatography techniques are available for analysis of the intact saponins (Kudou et al. The main complexity arises from the structures of the attached oligosaccharides. about the same as in soybeans. (1987). Toxicity was attributed to them simply by analogy with saponins from other sources that. are toxic.53 0 0.

glycetein. 2 Kitagawa et al. has an isoflavone profile approximating that of soybeans. Protein isolates contain reduced levels of isoflavones (600-1000 Mg/g)as compared with soybeans and flours as a result of the aqueous processing used during man ufacture. the isoflavones are present primarily as /3-glucosides and a portion of the glucosides also is substi tuted on the C-6 hydroxyl of the glucose by a malonyl group. Wang and Murphy 1994a. 2 Din = daidzin. In contrast. In the seed. nd = not detected. 0. Table 8 shows low and high values for isoflavone contents of soybean varieties reported by Wang and Murphy (1994b).31 0.26-0. for example. A concentrate made by aqueous alcohol ex traction is very low in isoflavones (73 Mg/g)because the isoflavones are soluble in aqueous alcohol and are thus largely removed during processing. tr = trace. Tofu is greatly reduced in isofla vones because of the aqueous processing during man ufacture. Gin = genistin. 1993). (1993) and Franke et al.25 Isoflavones Although long considered to be antinutritional fac tors. Coward et al. Roasted soybeans are low in the malonyl derivatives but higher in the acetyl forms as a result of the heat treatment.10 0. Gein = genistein. 1991 ). Wang and Murphy 1994b) but these may be degra dation products resulting from decarboxylation of the malonylisoflavones during extraction and workup of the extracts (Horowitz and Asen 1989). Granules and textured vegetable protein products contain appreciable quantities of the 6"-Oacetyl derivatives of genistin and daidzin. 1994b). . daidzein and glycetein) make up only 2% of the total isoflavones.COMPOSITIONAL CHANGES WITH SOYBEAN PROCESSING 585S TABLE 7 Supon i n content Product of Oriental soybean foods Saponin content g/100 g dry matter Soymilk1 Soymilk2 Yuba (dried soymilk film)2 Okara (residue from soymilk)2 Tofu2 Miso2 Natto2 1 Ireland et al.41 0. Additional data on flours. concentrates and isolates were reported by Eldridge (1982). Tempeh is somewhat lower in isoflavone Downloaded from jn.nutrition.15 0. these values range from 1200 to 4200 Mg/g-For additional information on variations of iso flavones with soybean varieties. although these workers did not report values for the acetylated or malonylated derivatives.30-0. which decarboxylates the malonyl glucosides. genistein and daidzein. Acetyl derivatives also have been reported (Farmakalidis and Murphy 1985. (1984). Isoflavone contents of traditional Oriental and Western soybean foods are summarized in Table 9. Glein = glycetein.39 0. The glucoside forms of the iso flavone predominate. and a minor one.33 0. because of their estrogenic properties soybean isoflavones are now of great interest because of their anticancer activities (see references in Coward et al. (1994). Soy flour. which represents only approximately 2% of the seed. made by defatting dehulled flakes and grinding. presumably because of heat treatment during processing. In the variety Pioneer 9111. (1986).org by on December 30. 6"-O-malonylgenistin accounts for 42% of the total followed by genistin (21%) and 6"-O-malonyldaidzin (16%). Dein = daidzein. especially in the hypocotyl (Kudou et al. see Eldridge and Kwolek (1983) and Wang and Murphy (1994b). the aglycones (genistein. Glin = glycetin. Soybeans contain two major isoflavones. crop year and location of growth. Beverage products approximate the com position for soybeans except for reduced levels of the malonyl derivatives. 2009 TABLE 8 products1*GlucosideProductVinton Isoflavone content of soybeans and processed protein soybeansPioneer 81 soybeansSoy 9111 flourSoy granuleTVPAProtein AProtein isolate BProtein isolate concentrateDin234637147727507tr88trGin32688840787063413730118Glin666041132146344931Din121690261106932018ndMalonylGin2901756102319319210088trG 1 Data from Wang and Murphy (1994a.

N. (1994) also report analyses for Ori ental and Western soy foods. nd = not detected. &Fenwick.. . including fat and water.. D. L. These changes may be intentional. I. soybean processing is useful and necessary to destroy or remove undesirable constituents. A. 58: 375-377. Biol. Dein daidzein. make nu trients more accessible or to improve palatability. LITERATURE CITED Beleia. T. Beleia. (1993) Lowering phytic phosphorus by hydration of soybeans. Gein = genistein. Similar trends are noted for bean paste (miso) and the other fermented soy foods. Price. Coward. R.586S SUPPLEMENT TABLE 9 Isoflavone content of traditional Oriental and Western soybean foods'1 ClucosideProductRoasted soybeansInstant AInstant beverage DTofuTempehBean beverage •159255ndndnd12tr256126nd671715GinMg/g63144259108164ndndnd425nd79trtr7637Glin724044n (miso|Honzukuri paste misoFermented curdSoy bean dogSoy hot baconTempeh burgerTofu yogurtSoy ParmesanCheddar ACheddar cheese BMozzarella cheese cheeseFlat noodleDin460444525252ml72ml35tr3642trtr167trGinMg/g551775745846596123tr672715880trml46336Glin6876758142118nd15141812nd121715ndMalonylDin453998 Downloaded from jn. (1990) Phosphorus and phytic acid distribution during soy milk processing. processing toward these ends also leads to changes in the composition of the various soybean materials compared with whole soybeans. e. K. T. S. T.g. The form may be altered by heat treatment and by enzyme reactions during fermentation but the isoflavones remain. and their /3-glycoside conjugates: antitumor isoflavones in soybean foods from American and Asian diets. Content of isoflavones in Western-style soy foods falls into the range of 43 ¿ig/g cheddar cheese-like for product to 386 jug/gfor tempeh burger. Curl.. Gin = genistin. & Barnes. as when isoflavones and saponins are extracted into ethanol during the washing required to produce some concentrates. C. K. Setchell.nutrition. Arq. Food Chem. I. (1985) The quantitative estimation of saponin in pea (Pisum sativum L. 18: 241-250. With the exception of the trypsin inhibitors. 2 Din = daidzin.) and soya (Glycine max). or they may be effected as a result of binding to the protein components throughout processing.Glin = glycetin. tr = trace. salt in miso. 388. However. It is apparent that processing generally does not re move the isoflavones from soybean protein products and foods. Agrie. R. The values for these foods are considerably lower than those of soy beans because soy is only one of several ingredients used. Food Sci. Food Chem.. Tecnol. (1993) and Dwyer et al. Barnes. the result of dif ferential solubilities. & Lethi. daidzein. Glein = glycetein. the compounds reviewed here gen erally are stable to processing of soybeans as practiced today. Ida. R. & Ida. J. L. 2009 ' Data from Wang and Murphy (1994a). as appears to occur with sa ponins and phytic acid. It should not therefore be difficult to maintain approximately the naturally occurring levels in the seed in many processed products if future studies dic tate that these compounds are desirable in our diet.. as in the case of heating to diminish trypsin inhibitor activity. except for concentrates prepared by alcohol extraction.. Coward et al. A. (1993) Genistein. L. content than tofu and contains elevated levels of the aglycones formed by enzymatic hydrolysis during fer mentation. 33: 623-629. by on December 30. Conclusions As is the case with many of the foods we consume today. Lowering of isoflavone contents of some soybean foods also results from dilution be cause of the addition of other ingredients. C. E. E. G. Thu Thao. 41: 1961-1967..

a Cheryan.. 28: 1197-1206. Crop Sci. Palamidis. Nutr. from Amer ican soybean. Bondi. 53: 867-871. Taniyama. 61:523-526. E. N. Food Chem. (1991) Malonyl isoflavone glycosides in soybean seeds (Glycine max Merrill). Food Sci. &. & Tacchini-Vonlanthen. Okubo. J. K.. Raboy. Omosaiye. (1983) Soybean isoflavones: effect of environment and variety on composition. (1986) Ultrastructural localization of glycinin and /3-conglycinin in Glycine max (soy bean) cv. & Reid. J. & Kearsley. 42: 1905-1913. M. E. S. Maple Arrow by the gold method. M. (1983) Nutrient composition of different varieties and strains of soybean. (1985) Isolation of 6"-O-acetylgenistin and 6"-O-acetyldaidzin from toasted defatted soyflakes. Price. protein concentrates. Kitagawa. O. mammals and cold blooded organisms. (1986) The saponin content and sapogenol composition of the seed of 13 varieties of legume. Tamur. E. A. a Taniyama. Food Biochem. A.nutrition. K. T. F. Sci. magnesium... (1984) Variation in seed total phosphorus. Kitagawa. D. J. M. Dziedzic. (Tokyo) 36: 2819-2828. Structure of soyasaponin A1. C. Cereal Chem. T. a Fenwick. T. Background. a bisdesmoside of soyasapogenol A. P. G. Cereal Chem. Tsukamoto. Agrie.. J. & Stanley. Plant Foods Hum. N. W. C. H. Int. Pharm. Agrie. Biotechnol. F. M. (1981) Factors affecting the nutritional quality of soya products.. Nutr. S. Curl. Pharm... Ishaaya. Kudou. & Liener. M.. T. J. Histochemistry85:291-294. Welti. (1983b) Ultrastruc tural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soybean) cv. Qual. S. Downloaded from jn. a Barnes. objectives. XLII. M. F. (1980) Determination of phytate in foods by phosphorus-31 Fourier transform nuclear magnetic resonance spectrometry. M. a Okubo. and A3. astringent par tially acetylated bisdesmosides of soyasapogenol A. iron and manganese contents of.. Crit. Am.S. J. & Trimble. 34: 186-191. New York. Kitagawa. (1979) Low-phytate. & Touchburn. W. Phytochemistry (Oxf) 28:2531-2532.. & Kwolek. Y. Fleury. T. Assoc. oats. M. Rackis. Cereal Chem. R. K. T. 37: 1185-1191. & Yoshikawa. Horowitz. (1983) Saponin content of food plants and some prepared foods. J. Taniyama. Br.. Nutr. T. Soc. Rackis. Eldridge. Horisberger. & Liener. Structures of acetyl-soyasponins AI. T. Y. (1981) Trypsin inhibitor activity of conventional foods which are pan of the British diet and some soya products. Magnolato. and isolates. J. Dickinson. zinc. (1972) Biochemical and nutritional assessment of different varieties of soybeans. J. M. I. E. 32: 273-278. 31: 139-150. Chem. &. A. J. L. and Zn availability from. J. M.. 41: 579-589. (1986) Protease inhibitors in plant foods: content and inactivation. Sakabe. R. Nati. & Fenwick. J. I. A. (1985a) Saponin and sapogenol. M. (1979) An evaluation of the phytate. Harland. Saito. D. D. I. (1984) Phytic acid and phosphorus content of various soybean protein fractions. 54: 606-609. J. S. 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