Wheat enzyme

Glutamate dehydrogenase Other enzymes Wheat Increase of activity Charest Phan, 1990... 

Com symps [8029-43 ] (glucose symp, starch symp) are concentrated solutions of partially hydrolyzed starch containing dextrose, maltose, and higher molecular weight saccharides. In the United States, com symps are produced from com starch by acid and enzyme processes. Other starch sources such as wheat, rice, potato, and tapioca are used elsewhere depending on avadabiHty. Symps are generally sold in the form of viscous Hquid products and vary in physical properties, eg, viscosity, humectancy, hygroscopicity, sweetness, and fermentabiHty. 

Cooking extmders have been studied for the Uquefaction of starch, but the high temperature inactivation of the enzymes in the extmder demands doses 5—10 times higher than under conditions in a jet cooker (69). Eor example, continuous nonpressure cooking of wheat for the production of ethanol is carried out at 85°C in two continuous stirred tank reactors (CSTR) connected in series plug-fiow tube reactors may be included if only one CSTR is used (70). 

EC 3.4.24.3]. Purified by using /V-ethylmaleimide to activate the enzyme, and wheat germ agglutinin-agarose affinity chromatography [Callaway et al. Biochemistry 25 4757 1986],... 

A different mechanism operates in the wheat germ enzyme. 2,3-Bisphosphoglycerate is not a cofactor. Instead, the enzyme carries out intra-molecular phosphoryl group transfer (Figure 19.25). The C-3 phosphate is transferred to an active-site residue and then to the C-2 position of the original substrate molecule to form the product, 2-phosphoglycerate. 

Mg2+ 21 g 0.35 g Activates enzymes for body processes Chocolate, nuts, instant coffee, wheat bran... 

The substitution pattern of arabinosyl side chains in AX from cereal flours and bran, based on the structural analysis of ohgomer fragments produced by xylan-degrading enzymes of known mode of action, was described by several authors [60-63], and various structural models were created [39,60]. fii a recent study [64] on the fine structure of wheat flour AX, a method was... 

In our investigations, we also detected the sorption of isoPO from potato, Arabidopsis and wheat, by calcium pectate. Moreover, we observed the binding with calcium pectate of potato PO from the fraction of proteins ionically bound with cell walls. It is likely that the ability of some PO isoforms to bind with pectin ensures the spatial proximity of these enzymes to the sites of the initiation of lignin synthesis and that these "pectin-specific" isoforms take part in this process. 

Mayoral, M.L., Atsmon, D., Gromet-Elhanan, Z. Shimshi, D. (1981). Effect of water stress on enzyme activities in wheat and related wild species Carboxylase activity, electron transport and photophosphorylation in isolated chloroplasts. Australian Jourrml of Plant Physiology, 8, 385-94. 

Pectins were extracted from isolated cell walls of 5-week-old wheat plants using different methods. Enzymic digestions of the cell walls involved pectinases such as a commercial pectolayse or recombinant endopolygalacturonase [Maness Mort, 1989]. Chemical extractions involved the chelating agent imidazole [Mort et al., 1991] or solvolysis with anhydrous HF at 0 °C in a closed teflon line [Mort et al., 1989] followed by imidazole extraction. 

Solutions of different pectic substances were injected into healthy wheat plants, with or without the glycoproteogalactan elicitor, and the activities of the enzymes PAL and POD were determined. These enzymes are involved in the hypersensitive reaction of wheat against the rust fungus, and increased activities can be expected after elicitation, whereas suppressor active substances will cause a reduction of the elicitor-induced enzyme activities. 

Portions (50 mU MCA-hydrolsing activity) of purified CinnAE were incubated at 37°C with SBP (10 mg), both in the presence and absence of other carbohydrases, in 100 mM MOPS (pH 6.0) in a final volume of 1 mL. Incubations containing boiled enzyme were performed as controls. Reactions were terminated by boiling (3 min) and the amount of free ferulic acid determined using a method described previously for de-starched wheat bran [18]. The total amount of alkali-extractable ferulic acid present in the SBP was 0.87% [5]. 

When Rhizopus sp. 26R was cultivated in the solid substrates without addition of rice bran but composed of only wheat bran and rice husk at the ratio of 18 2. The pectinase activity from the culture was approx. 25-35 unit/ml within 2 days and the production remained constant for 4 days (Figure 3). One gram of raw starch from cassava tuber, 1 g of pectin or 0.5 g of yeast extract was added to the solid substrates in order to induce higher activity of the enzsrme. The results showed that either 1 g raw cassava starch or 1 g pectin that was added to the 20 g solid substrates increased the enzyme activity to 1.7 and 2.4 times, respectively (Figure 3). The production of pectinase in soHd substrates with wheat bran and rice husk could be enhanced with the addition of raw cassava starch and pectin. 

Addition of rice bran to the solid substrates to make the ratio of wheat bran, rice bran and rice husk to 9 9 2 helped increasing the activity of pectinases from Rhizopus sp. 26R as shown in Figure 4. The activity of the enzyme was approx. 4.3 times higher. Moreover, either 1 g of pectin or 0.5 g of yeast extract did not help increasing of the enzyme production. In contrary, the enz5mie activity was decreased 2.6 times to that of the former one. Addition of raw cassava starch to the substrates did no effect to the enzyme production (data not shown). 

Different ratios of the solid substrates, wheat bran, rice bran and rice husk, were done and the activity of the pectinases was compared in Figure 5. The mixture of wheat bran, rice bran and rice husk in the ratios of 9 9 2 or 6 12 2 appeared to be two of the best composition ratios for growth of the fungus and the pectinase production.The ratio of 6 12 2 was selected for the enzyme production since rice bran was cheaper than wheat bran and locally obtained. 

Figure 6,7 and 8 showed the results of the pectinase activity when produced in the solid substrates containing wheat bran, rice bran and rice husk in the ratio of 6 12 2. The highest activity obtained when the strain was grown on the solid substrates with 58 % initial moisture content, pH adjusted to 5.7 and incubation temperature was at 32°C. Under these conditions, the highest activity of the enzyme that could be obtained from Rhizopus sp. 26R was ca. 700 units of enzyme activity per gram of solid substrates. 

The enzyme production in the solid substrates composed of wheat bran and rice husk (18 2) could be increased by the addition of either 1 g raw cassava starch or 1 g pectin to a 20 g substrates. The enzyme activity increased approx. 1.7 and 2.4 times, respectively. 

Addition of rice bran to the mixture of wheat bran and rice husk was the best substrates for the fungal pectinase production. The solid substrates that composed of wheat bran, rice bran and rice husk at the ratio of 6 12 2 was selected to be the best since rice bran are easily found in South-east Asian countries. Addition of either raw cassava starch or pectin as inducer is not needed. On the otherhand, pectin even inhibited the activity of the enzyme as well as that reported by Elegado and Fujio (6). 

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