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Beans proteins

Flours % Crude Protein % Bean Flour 5 Required for Nitrogen Balance... [Pg.244]

Sources. Zinc is found in oysters, and to a far lesser degree in most animal proteins, beans, nuts, almonds, whole grains, pumpkin seeds, and sunflower seeds. [Pg.269]

Urease is one of the enzymes which have been obtained in the crystalline state. This has been done by stirring jack bean meal with 30°o aqueous acetone, filtering and allowing the filtrate to remain at o for several hours. The urease which crystallises out is separated by centrifuging and is then recrystallised. Like crystalline pepsin and trypsin, it is a protein. [Pg.519]

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). [Pg.156]

The mmen is not functional at birth and milk is shunted to the abomasum. One to two weeks after birth, the neonate consumes soHd food if offered. A calf or lamb that is nursing tends to nibble the mother s feed. An alternative method of raising the neonate is to remove it from its mother at a very young age, <1 week. A common example of an early weaning situation is the dairy calf that is removed from the cow soon after birth so that the cow s milk supply might be devoted entirely to production. In this instance, the neonate requires complete dietary supplementation with milk replacer. Sources of milk replacer protein have traditionally included milk protein but may also include soybean proteins, fish protein concentrates, field bean proteins, pea protein concentrates, and yeast protein (4). Information on the digestibiUty of some of these protein sources is available (4). [Pg.157]

Investigations have focused on the content of polyphenoHcs, tannins, and related compounds in various foods and the influence on nutrient availabiHty and protein digestibiHty. It has been estabHshed that naturally occurring concentrations of polyphenoloxidase and polyphenols in products such as mushrooms can result in reduced iron bio availabiHty (75). Likewise, several studies have focused on decreased protein digestibiHty caused by the tannins of common beans and rapeseed (canola) (76—78). [Pg.479]

Currently available proteins are all deficient to greater or lesser extent in one or more of the essential amino acids. The recently advanced plastein reaction (229) has made it possible to use protein itself as substrate and to attach amino acid esters to the protein with high efficiency. By this method, soy bean protein (which is deficient in methionine) has been improved to the extent of having covalently attached L-methionine at 11%. [Pg.296]

Other Lethal Agents. There are a number of substances, many found in nature, which are known to be more toxic than nerve agents (6). None has been weaponized. Examples of these toxic natural products include shellfish poison, isolated from toxic clams puffer fish poison, isolated from the viscera of the puffer fish the active principle of curare "heart poisons" of the digitaUs type the active principle of the sea cucumber active principles of snake venom and the protein ricin, obtained from castor beans (See Castor oil). [Pg.399]

Although flavor precursors in the unroasted cocoa bean have no significant chocolate flavor themselves, they react to form highly flavored compounds. These flavor precursors include various chemical compounds such as proteins, amino acids, reducing sugars, tannins, organic acids, and many unidentified compounds. [Pg.91]

The natural moisture of the cocoa bean combined with the heat of roasting cause many chemical reactions other than flavor changes. Some of these reactions remove unpleasant volatile acids and astringent compounds, partially break down sugars, modify tannins and other nonvolatile compounds with a reduction in bitterness, and convert proteins to amino acids that react with sugars to form flavor compounds, particularly pyrazines (4). To date, over 300 different compounds, many of them formed during roasting, have been identified in the chocolate flavor (5). [Pg.91]

Ricin (toxin from Castor bean Ricinus communis) [A chain 96638-28-7 B chain 96638-29-8] Mr -60,000, amorphous. Crude ricin, obtained by aqueous extraction and (NH4)2S04 pptn, was chromatographed on a galactosyl-Sepharose column with sequential elution of pure ricin. The second peak was due to ricin agglutinin. [Simmons and Russell Anal Biochem 146 206 1985.) Inhibitor of protein synthesis. EXTREMELY DANGEROUS, USE EXTREME CARE [instructions accompany product]. [Pg.565]

A nucleic acid can never code for a single protein molecule that is big enough to enclose and protect it. Therefore, the protein shell of viruses is built up from many copies of one or a few polypeptide chains. The simplest viruses have just one type of capsid polypeptide chain, which forms either a rod-shaped or a roughly spherical shell around the nucleic acid. The simplest such viruses whose three-dimensional structures are known are plant and insect viruses the rod-shaped tobacco mosaic virus, the spherical satellite tobacco necrosis virus, tomato bushy stunt virus, southern bean mosaic vims. [Pg.325]

Of these materials zein, the maize protein, has been used for plastics on a small scale. It can be cross-linked by formaldehyde but curing times are very long. Complicated bleaching processes have led to the production of almost colourless samples in the laboratory but the process cannot readily be extended to large-scale operation. The cured product has a greater water resistance than casein. Proteins from soya bean, castor bean and blood have also been converted into plastic masses but each have the attendant dark colour. [Pg.860]

Protein is an important component of most foods. Nearly everything we eat contains at least a small amount of protein. Lean meats and vegetables such as peas and beans are particularly rich in protein. In our digestive system, proteins are broken down into small molecules called a-amino acids. These molecules can then be reassembled in cells to form other proteins required by the body. [Pg.621]

Some members of the Liliaceae accumulate free azetidine-2-carboxylic acid in a much higher concentration than that found to be lethal to mung bean seedlings, but it is not incorporated into their proteins. Fowden (43) postulated that these plants either had a proline-incorporating system which was more specific than that found in other species, or some subcellular mechanism operated to prevent the homolog from reaching the sites involved in protein synthesis. Data which supported the first suggestion were subsequently obtained (116). [Pg.129]

In addition to effects on biochemical reactions, the inhibitors may influence the permeability of the various cellular membranes and through physical and chemical effects may alter the structure of other subcellular structures such as proteins, nucleic acid, and spindle fibers. Unfortunately, few definite examples can be listed. The action of colchicine and podophyllin in interfering with cell division is well known. The effect of various lactones (coumarin, parasorbic acid, and protoanemonin) on mitotic activity was discussed above. Disturbances to cytoplasmic and vacuolar structure, and the morphology of mitochondria imposed by protoanemonin, were also mentioned. Interference with protein configuration and loss of biological activity was attributed to incorporation of azetidine-2-carboxylic acid into mung bean protein in place of proline. [Pg.139]

Biotin can be synthesized by the human colon flora. The question to which extent this production contributes to covering the host-organism s requirements is, however, subject to discussion. In most foods of animal origin as well as in cereals, biotin prevails in the protein (= enzyme)-bound form as e-N-biotinyl-L-lysine (= biocytin). Brewer s yeast, liver, soya beans, and peanuts number among the biotin rich foods [1]. [Pg.270]

If the objective were to maximize energy production in producing food, all efforts would go toward grain and bean production where five times the energy is produced as is used, or to the extreme, do all the tasks manually in which 30 to 40 times the energy is produced as used. In the later case, all the able-bodied men, women, and children would be needed to produce the food now available. In that scenario we would also deny our diet of the variety of leafy vegetables, fruits and nuts for fiber and vitamins, and animal and fish products for a variety of proteins. [Pg.333]

Bean hypocotyls (Phaseolus vulgaris) incision woimding of hypocotyls oxidative cross-linking of cell wall proteins [176]... [Pg.171]

Gianazza, E Miller, I Eherini, I Castiglioni, S, Low-Tech Electrophoresis, Small bnt Bean-tifnl, and Effective Electrophoretic Titration Cnrves of Proteins, Electrophoresis 20, 1325, 1999. [Pg.612]

Dry bean curd refuse was used as the substrate in the lactic acid fermentation with simultaneous saccharification (SSF). The dry bean curd refuse was preliminarily sieved under a mesh size of 250 II m. It contained 12.3% water, 4.0% ash, 0.8% lipid, 29.3% protein, 53.6% carbohydrate, respectively, in weight basis. The cellulase derived from Aspergilltis niger with an enzymatic activity of 25,000 units/g (Tokyo Kasei Industry Inc.) was employed as the saccharification enzyme. [Pg.133]

CARVALHO M R, SGARBiERi V 0 (1998) Relative importance of phytohemagglutinin (lectin) and trypsin-chymotrypsin inhibitor on bean (Phaseolus vulgaris L) protein absorption and utilization by the rat. JNutr Sci Vitaminol (Tokyo). 44 685-96. [Pg.177]

ISHIMOTO M, YAMADA T, KAGA A (1999) Insecticidal activity of an alpha-amylase inhibitor-like protein resembling a putative precursor of alpha-amylase inhibitor in the common bean, Phaseolus vulgaris L. Biochim Biophys Acta. 1432 104-12. [Pg.179]

MYER R o, FROSETH J A, COON 0 N (1982) Protein utilization and toxic effects of raw beans (Phaseolus vulgaris) for young pigs. . 1 Anim Sci. 55 1087-98. [Pg.182]


See other pages where Beans proteins is mentioned: [Pg.512]    [Pg.513]    [Pg.515]    [Pg.532]    [Pg.577]    [Pg.512]    [Pg.513]    [Pg.515]    [Pg.532]    [Pg.577]    [Pg.346]    [Pg.468]    [Pg.470]    [Pg.476]    [Pg.476]    [Pg.433]    [Pg.99]    [Pg.296]    [Pg.447]    [Pg.447]    [Pg.105]    [Pg.9]    [Pg.129]    [Pg.129]    [Pg.138]    [Pg.598]    [Pg.250]    [Pg.31]    [Pg.46]    [Pg.333]    [Pg.176]    [Pg.178]   
See also in sourсe #XX -- [ Pg.126 , Pg.127 , Pg.128 , Pg.129 , Pg.130 , Pg.131 , Pg.132 , Pg.133 , Pg.134 , Pg.135 ]




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