Enzyme soybean

Other plants such as potatoes, cauliflower, cherries, and soybeans and several fungi may also be used as sources of peroxidase enzymes. Soybeans, in particular, may represent a valuable source of peroxidase because the enzyme is found in the seed coat, which is a waste product from soybean-based industries [90]. In this case, it may be possible to use the solid waste from the soybean industry to treat the wastewaters of various chemical industries. In fact, the direct use of raw soybean hulls to accomplish the removal of phenol and 2-chlorophenol has been demonstrated [105]. However, it should be noted that this type of approach would result in an increase in the amount of solid residues that must be disposed following treatment. Peroxidases extracted from tomato and water hyacinth plants were also used to polymerize phenolic substrates [106], Actual plant roots were also used for in vivo experiments of pollutant removal. The peroxidases studied accomplished good removal of the test substrate guaiacol and the plant roots precipitated the phenolic pollutants at the roots surface. It was suggested that plant roots be used as natural immobilized enzyme systems to remove phenolic compounds from aquatic systems and soils. The direct use of plant material as an enzyme source represents a very interesting alternative to the use of purified enzymes due to its potentially lower cost. However, further studies are needed to confirm the feasibility of such a process. 

The enzyme, soybean lipoxygenase-1 (SLO), offers an excellent system in which to illustrate the power of Eq. (10.20) in reproducing experimental data. Several characteristics of SLO are impossible to interpret through a Bell-like tunneling correction. The KIE on k at, k at = 81 + 5, is nearly temperature independent,... 

Raw soybeans also maybe used as a supplemental protein source. Dry beans, ie, beans normally harvested in the green / imm a tiire state, fava beans, lupins, field peas, lentils, and other grain legumes are potential supplemental protein sources however, several of these may have deleterious effects, predominantly enzyme inhibition, on the animal. The supply of each is limited (5). 

Hydrolyzed Vegetable Protein. To modify functional properties, vegetable proteins such as those derived from soybean and other oil seeds can be hydrolyzed by acids or enzymes to yield hydrolyzed vegetable proteins (HVP). Hydrolysis of peptide bonds by acids or proteolytic enzymes yields lower molecular weight products useful as food flavorings. However, the protein functionaHties of these hydrolysates may be reduced over those of untreated protein. 

Other experiments with Gibberellafujikuroi the fungus that produces gibbereUin, indicate that GA production is blocked by BAS 111. Very detailed and carehil experiments conducted with enzymes in ceU-free systems strongly support this mode of action, ie, using /-kaurene oxidase and cinnamate 4-mono-oxygenase isolated from pea apices and soybean suspension cells, and avanone-2-hydtoxylase and dibydroxypterocarpane 6-hydtoxylase from soybean suspension cells (31). 

Arachin, the counterpart of glycinin in peanuts, consists of subunits of 60,000—70,000 mol wt which on reduction with 2-mercaptoethanol yield polypeptides of 41,000—48,000 and 21,000 mol wt (17) analogous to the behavior of glycinin. In addition to the storage proteins, oilseeds contain a variety of minor proteins, including trypsin inhibitors, hemagglutinins, and enzymes. Examples of the last are urease and Hpoxygenase in soybeans. 

Lipoxygenase-Catalyzed Oxidations. Lipoxygenase-1 catalyzes the incorporation of dioxygen into polyunsaturated fatty acids possessing a l(Z),4(Z)-pentadienyi moiety to yield ( ),(Z)-conjugated hydroperoxides. A highly active preparation of the enzyme from soybean is commercially available in purified form. From a practical standpoint it is important to mention that the substrate does not need to be in solution to undergo the oxidation. Indeed, the treatment of 28 g/L of linoleic acid [60-33-3] with 2 mg of the enzyme results in (135)-hydroperoxide of linoleic acid in 80% yield... 

Koch, G., Wells, R. Grisebach, H. (1987). Differential induction of enzyme in soybean cell cultures by elictor or osmotic stress. Planta, 171, 519-24. 

There is evidence that protease inhibitors selectively regulate the activity of specific digestive enzymes at the level of gene expression (Rosewicz et al., 1989). Specifically, soybean trypsin inhibitor increases secretion of proteases, including a form of trypsin that is resistant to inhibition but does not cause an increase in amylase secretion. Although the relationships between protease inhibitors and exocrine pancreatic secretion have received the most attention, pancreatic secretion is increased when potato fiber is added to the diet (Jacob et al., 2000), although the mechanism and signaling pathway have not been elucidated. 

KROGDAHL A, HOLM H (1981) Soybean proteinase inhibitors and human proteolytic enzymes selective inactivation of inhibitors by treatment with human gastric juice. /M/fr. Ill 2045-51. 

ROSEWicz s, LEWIS L D, WANG X Y, LiDDLE R A, LOGSDON c D (1989) Pancreatic digestive enzyme gene expression effects of CCK and soybean trypsin inhibitor. dm J Physiol. 256 G733-8. 

Bartley, G.E. et al.. Molecular cloning and expression in photosynthetic bacteria of a soybean cDNA coding for phytoene desaturase, an enzyme of the carotenoid biosynthesis pathway, Proc. Natl. Acad. Sci. USA 88, 6532, 1991. 

Morishita, N., Kamiya, K., Matsumoto, T., Sakai, S., Teshima, R., Urisu, A., Moriyama, T., Ogawa, T., Akiyama, H., and Morimatsu, F. (2008). A reliable enzyme-linked immunosorbent assay for determination of soybean proteins in processed foods. /. Agric. Food Chem. 56, 6818-6824. 

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