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Formed from Proteins

Since the 1980s, the number of academic research programmes and industrial research and development projects on protein-based bioplastics have increased exponentially, as a result of the present interest in using some field crops for renewable and biodegradable materials for non-food applications, and also in order to explore the unique specific properties of proteins. The complexity of proteins and the diversity of their different fractions can be tapped to develop materials with original functional features that differ markedly from those of standard synthetic plastic materials. Apart from the previously mentioned proteins. [Pg.339]

Pood packaging (dried foods, short life cycle food, egg boxes, fresh or minimally processed fruits and vegetables, dairy products, organically grown products, etc.) [Pg.340]

Paper or cardboard (windows from paper envelopes or for cardboard packaging, coating for paper or cardboard) [Pg.340]

Hygienic disposable (nappies, sanitary napkins, sticks for cotton swabs, razors, toothbrushes, etc.) [Pg.340]

Miscellaneous short life goods (pens, toys, gadgets, keys holders, etc.) [Pg.340]


If allowance is made for the fact that much of the carbohydrate formed from protein, which is oxidized in the non-diabetic, may escape metabolism by the diabetic and be excreted in the urine, the protein R. Q. for the diabetic should be 0.632 instead of the normal value of 0.802.134 The R. Q. for fat is also altered because of the failure of a complete combustion of this foodstuff, due to the attendant ketonuria. [Pg.155]

Aminoacyl adenylates (296), which are formed from protein amino acids and ATP, act as acylating agents towards t-RNAs, acylating their terminal 3 -hydroxy groups. These charged tRNAs are then used in protein synthesis. Little is known about the reactivity of aminoacyl adenylates (296), and studies are now reported of a model compound, alanyl ethyl phosphate (297). As expected, hydrolysis in both acid and base involves attack at the C=0 group of (297) with departure of ethyl phosphate. Metal ions (Cu +, Zn +) were found to act as catalysts of the hydrolysis. [Pg.89]

Coke, M., Wilde, P.J., Russell, E.J., Clark, D.C. (1990). The influence of surface composition and molecular diffusion on the stability of foams formed from protein detergent mixtures. Journal of Colloid and Interface Science, 138, 489-504. [Pg.346]

Other Protein Components. Other protein components In complex food systems and In protein Ingredient preparations may Interfere with or modify gelation reactions. Protein Interaction between whey protein and casein upon heating has a profound Influence on the characteristics of the casein gel structure In cheesemaking. Similarly protein Interactions are Important to meat structures. Protein-protein Interaction between soy and meat proteins has also been demonstrated with heat treatment (28). While concrete Interaction data have not been collected on protein gels formed from protein combinations, gelation properties of whey proteln/peanut flour blends have been Investigated GU) ... [Pg.138]

Some membranes contain relatively large pores which allow for the free passage of molecules with molecular weights up to about 600. For example the outer membranes of gram negative bacteria contain pores with diameters of about 10 A which are formed from proteins called porins. [Pg.408]

Rideal and his collaborators found that solid particles of protein spread very rapidly on a clean surface their method of spreading is to coat a quartz fibre, first covered with paraffin wax, with a little protein this is dipped into the water surface, and the amount of protein passing into the surface ascertained by weighing the fibre on a simple micro-balance.1 By this method somewhat larger areas can sometimes be obtained, and films formed from proteins which cannot be made to form homogeneous films when spread by Gorter s technique and in certain cases the average thickness of the fully spread film is only about 3 A. [Pg.87]

Members of tbe amyloid family bave no sequence homology with each other, but fibers formed from proteins in tiiis group share a similar secondary structure. Two characteristic reflections (at 10 and 4.8 A) are produced when fibers formed from any of the amyloid proteins are analyzed by x-ray diffraction (Sunde et al, 1997). This pattern defines the cross P-pleated sheet structure in which P sheets lie parallel to the long axis of the fiber, with tbe strands of each sheet oriented perpendicular to the fiber axis (Sunde et al, 1997). Fibers formed from tbe NM region of Sup35 share tbis structure (Serio etal, 2000) thus, Sup35 can be defined as an amyloidogenic protein. [Pg.347]

In the field of research methods probably the most important application of protein surfactant complexation is in the technique of polyacrylamide gel electrophoresis in the presence of SDS, the so-called SDS-PAGE technique, used for the analysis and estimation of molecular masses of protein subunits [22], Protein subunit-SDS complexes are formed from proteins reduced by /3-mercaptoethanol to remove disulphide bonds. The binding of SDS to the polypeptide chains oc-... [Pg.240]

Many other glucosinolates appear to arise by modification of glucosinolates formed from protein amino acids at the glucosinolate stage or are derived from nonprotein amino acids (Larsen, 1981). [Pg.303]

Pfliiger revived Liebig s theory he showed that fats can be formed from proteins in the body. [Pg.316]

The determination of o-tyrosine (formed from proteins during irradiation) can be done with HPLC as well as with GC. There are no satisfactory methods because of the bad resolution in the chromatograms, interfering sample constituents and missing reference materials. This area of irradiation analysis will be of further interest in the future because of identification problems with low-fat-containing protein-rich foodstuffs. [Pg.262]

Although the free iron is catalytically active, the relative importance of protein-bound iron is being debated. Lipid oxidation in cooked meat is not only attributed to changes in iron distribution by protein denaturation and the release of catalytically active non-heme iron, but also to the disruption of cell membranes in meat that brings the polyunsaturated hpids in close contact to the catalysts. Unfortunately, in many studies using the TBA test to determine the effects of different forms of iron on lipid oxidation in meats, the results must be interpreted with caution, because the TBA reaction is significantly affected by iron and other metals, and is subject to serious interference by other factors. In addition to products of lipid oxidation, TB ARS are also formed from proteins and nucleic acids and other non-lipid components in meat tissues that confound the results of the TBA test. [Pg.331]

A process of treating a product synthetically formed from protein material to improve or modify the dyeing affinities, resistance to water and chemicals, and other properties... [Pg.407]


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Amino acids proteins formed from

Material Formed from Proteins

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