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Soybean purification

KOCHS, G., GRISEBACH, H., Phytoalexin synthesis in soybean purification and reconstitution of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase and separation from cytochrome P450 cinnamate 4-hydroxylase. Arch Biochem. Biophys., 1989,273,543-553. [Pg.28]

Fischer, D. et al. (1990) Phytoalexin synthesis in soybean purification and characterization of NADP H 2 -hydroxydaidzein oxidoreductase... [Pg.162]

Trower MK, FS Sariaslani, DP O Keefe (1989) Purification and characterization of a soybean flour-induced cytochrome P-450 from Streptomyces griseus. J Bacteriol 171 1781-1787. [Pg.89]

The plant of choice which can be used for PHA production will be influenced by a number of factors. Of prime importance is cost, i. e., in which crop will PHA production be cheapest. The answer to this question is likely to be different depending on the agricultural economics of each country. For example, if one considers oilseed crops, rapeseed may be the best crop for Northern European countries and Canada, sunflower for Southern European countries, and soybean for the USA. Other important factors which may influence the choice of target plant are the nature of the metabolic pathway that needs to modified for synthesis of a particular PHA, the procedure used for PHA purification, and the other uses of the crop besides PHA production. [Pg.231]

In the quest to find other plants that are suitable as bioreactors, various monocoty-ledonous and dicotyledonous species have been tested. These include corn [16], rice and wheat [17], alfalfa [18], potato [19, 20], oilseed rape [21], pea [22], tomato [23] and soybean [24]. The major advantage of cereal crops is that recombinant proteins can be directed to accumulate in seeds, which are evolutionar specialized for storage and thus protect proteins from proteolytic degradation. Recombinant proteins are reported to remain stable in seeds for up to five months at room temperature [17] and for at least three years at refrigerator temperature without significant loss of activity [25]. In addition, the seed proteome is less complex than the leaf proteome, which makes purification quicker and more economical [26]. [Pg.92]

Bednar RA, Hadcock JR (1988) Purification and characterization of chalcone isomerase from soybeans. J Biol Chem 263(20) 9582-9588... [Pg.90]

Yang, F., Ma, Y., and Ito, Y., Separation and purification of isoflavones from a crude soybean extract by high-speed countercurrent chromatography, J. Chromatogr. A, 928, 163, 2001. [Pg.34]

Materials and Methods. Fully deuterated phycocyanin and protio phycocyanin from Ph. luridum were used. The method of purifying phycocyanin was identical to that used previously (15, 16). The purity of the phycocyanin preparations, the complete substitution of deuterium for hydrogen in the fully deuterated phycocyanin, and the reversibility of the aggregation phenomenon were ascertained as previously (4, 16). Purified bovine trypsin, soybean trypsin inhibitor, and bovine liver catalase were obtained from the Worthington Biochemical Corp., Freehold, N. J., and used without further purification. Bovine a -casein B was kindly supplied by Chien Ho of the University of Pittsburgh. [Pg.29]

Wegenmayer, H., Ebel, J. and Grisebach, H., 1976, Enzymic synthesis of lignin precursors Purification and properties of a cinnamoyl-CoA NADPH reductase from cell suspension cultures of soybean (Glycine max L.), Eur. J. Biochem. 65 529-536. [Pg.148]

Streit, L., Martin, B.A. Harper, J.E. (1987). A method for the separation and purification of the three forms of nitrate reductase present in wild-type soybean leaves. Plant Physiology 84, 654-7. [Pg.76]

W-R Shieh. Part I. Studies on the active site-directed enzyme inhibitors of soybean lipoxygenase. Part n. Purification and studies on the [i-keto ester reductases from baker s yeast. Ph.D thesis. University of Wisconsin, Madison, WI, 1987. [Pg.206]

Partially purified soybean hemagglutinin was prepared from untoasted soybean flour (Soyafluff 200W, Central Soya, Chicago, IL) according to the method of Liener (11). Final purification was achieved by chromatography on hydroxylapatite, prepared Current address Research Division. Science Park, Smithville, TX 78957. [Pg.67]

Gonzalez, R., Polo, F., Zapatero, L., Caravaca, F., Carreira, J. 1992. Purification and characterization of major inhalant allergens from soybean hulls. Clin Exp Allergy 22 748-755. [Pg.289]

Sharp, J. K., Valent, B., and Albersheim, P. 1984. Purification and partial characterization of a P-glucan fragment that elicits phytoalexin accumulation in soybean. J. Biol. Chem. 259, 11312-11320... [Pg.362]

Nagao, T., Kobayashi, T., Hirota, Y., Kitano, M., Kishimoto, N., Fujita, T., Watanabe, Y., and Shimada, Y. 2005. Improvement of a process for purification of tocopherols and sterols from soybean oil deodorizer distillate. J. Mol. Catal. B Enzym., 37, 56-62. [Pg.80]

Shimada, Y., Nakai, S., Suenaga, M., Sugihara, A., Kitano, M., and Tominaga, Y. 2000. Facile purification of tocopherols from soybean oil deodorizer distillate in high yield using lipase. /. Am. Oil Chem. Soc., 77,1009-1013. [Pg.81]

Additions of valine, leucine, and isoleucine were found to relieve the growth inhibitory effects of TP on Bacillus cell cultures, soybean cell cultures, and Arabidopsis seedlings. ALS isolated from a number of sources was found to be sensitive to TP at nM levels. The barley enzyme has been amenable to purification. A purification procedure that gives >60 % recovery and 235-fold purification is described. [Pg.270]

Phillippy, B.Q., Ullah, A.H.J., and Ehrlich, K.C., 1994, Purification and some properties of inositol 1,3,4,5,6-pentaHsphosphate 2-kinase from immature soybean seeds. J. Biol. Chem. 269 28393-28399. [Pg.100]

Dalton, D. A., Langeberg, L., and Robbins, M., 1992, Purification and characterisation of mondehydroascorbate reductase from soybean root nodules. Arch. Biochem. Biophys. 292 281n286. [Pg.343]

Considerable purification of lipoxygenase from soybeans was achieved by Balls et al (15), They used conventional protein purification methods and the carotene oxidase reaction to follow the enzyme activity. Theorell et al, (16), in 1947, crystallized the enzyme, or more correctly, one of the several isoenzymes in soybean. We believe this was lipoxygenase-1 as described later. [Pg.325]

Soy lecithin is a coproduct of oil processing. As a result, purification steps used to produce quality oil may affect the lecithin components. Also, soybeans exposed to frost damage, or subjected to prolonged storage, have reduced lecithin yields (33). Phospholipases, which produce phosphatidic acid, are active during storage and may reduce the yield of lecithin (34). During the maturation process, the major phospholipids (PC, PE, and PI) increase, and others decrease or remain constant (32). [Pg.1724]

S.3.2.2. Pretreatment for Fractionation and Anaiyticai Purposes Chemical reactions can be used to modify the composition of a lipid mixture to facilitate its fractionation. As mentioned previously, such approaches have been employed in the fractionation of soybean (117) and olive oil deodorizer distillates (87) and fish oils (97). However, although the fractionation steps in these studies were carried out under supercritical conditions, the use of SCCO2 as a reaction medium in the pretreatment reactions has not been explored. Gunnlaugsdottir et al. (151, 165-168) investigated the alcoholysis of cod liver oil in SCCO2 for the concentration of fatty acids such as EPA and DHA. A process for the purification of polyunsaturated fatty acids from biomass on an analytical scale using in situ SEE/SCF reaction and chromatography has been patented (215). [Pg.2829]


See other pages where Soybean purification is mentioned: [Pg.226]    [Pg.124]    [Pg.412]    [Pg.226]    [Pg.259]    [Pg.613]    [Pg.894]    [Pg.1228]    [Pg.92]    [Pg.68]    [Pg.133]    [Pg.146]    [Pg.79]    [Pg.137]    [Pg.138]    [Pg.233]    [Pg.258]    [Pg.382]    [Pg.340]    [Pg.331]    [Pg.1737]    [Pg.2720]    [Pg.2815]    [Pg.2856]   
See also in sourсe #XX -- [ Pg.35 , Pg.232 ]




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