Enzymes modifications

AMINOACIDS - L-MONOSODIUMGLUTAMATE (MSG)] (Vol 2) -enzyme modification pNZYME APPLICATIONS - INDUSTRIAL] 0/ol9) -in meat products [MEAT PRODUCTS] (Vol 16)... 

The widely commercially exploited guar GaM has been the subject of some studies dealing with chemical or enzymic modifications aimed to extend the apphcation range of this polysaccharide. Specific oxidation on the C-6 position of the Galp side chain units was performed by /1-galactosidase [241,430]. 

The structural varieties of hemicelluloses offer a number of possibilities for specific chemical, physical, and enzymic modifications. Future advancements will be based on the synthesis of hemicellulose-based polymers with new functionalities and with a well-defined and preset primary structure both on the level of the repeating imit and the polymer chain. Hemicelluloses have also started to be attractive to synthetic polymer chemists as... 

Martirosova, E., Karpekina, T., El -Registan, G. Enzyme modification by natural chemical chaperons of microorganisms. Microbiology, Vol.73, No.5, (August 2004), pp. 609-615, ISSN 1350-0872... 

Target tissue response Synthesis of new enzymes Modification of existing enzymes Synthesis of new enzymes Modification of existing enzymes... 

Figure 27.1 Three common nucleoside triphosphate derivatives that can be incorporated into oligonucleotides by enzymatic means. The first two are biotin derivatives of pyrimidine and purine bases, respectively, that can be added to an existing DNA strand using either polymerase or terminal transferase enzymes. Modification of DNA with these nucleosides results in a probe detectable with labeled avidin or streptavidin conjugates. The third nucleoside triphosphate derivative contains an amine group that can be added to DNA using terminal transferase. The modified oligonucleotide then can be labeled with amine-reactive bioconjugation reagents to create a detectable probe.

Enzyme modification, performance improvement, 3 671 Enzyme multiplied immunological technique (EMIT), 12 97 Enzyme Nomenclature, 17 402 Enzyme-product (EP) complex, 10 318 Enzyme production, Bacillus and, 12 477 Enzymes. See also Restriction enzymes Enzymes, 5 201... 

For some recent reviews on enzyme modification see (a) Reetz, M.T., Evolution in the test-tube as a means to creat selective biocatalysts. Chimia, 2007,61, 100-103 (b) Sylvestre, J., Chautard, H., Cedrone, E. and Delcourt, M., Directed evolution of biocatalysts. Org. Proc. Res. Dev., 2006, 10, 562-571 (c) Hibbert, E.G. and Dalby, P.A., Directed evolution strategies for improved enzymatic performance. Microb. Cell Fact., 2004, 4, 29 (d) Otten, L.G. and Quax, W.J., Directed evolution selecting today s biocatalysts. Biomol. Eng., 2005, 22, 1-9. 

Further, drug absorption, distribution, and elimination from the body may vary due to differences in protein binding, enzymic modification, etc, since proteins are also chiral entities (see Chapter 13). 

After donating its phosphate group to ADP, 1,3-diphosphoglycerate is converted into 3-phospho-glycerate. This reaction is followed by enzymic modification to 2-phosphoglycerate. 

Preisig-Mueller, R. et al.. Plant polyketide synthases leading to stilbenoids have a domain catalyzing malonyl-CoA C02 exchange, malonyl-CoA decarboxylation, and covalent enzyme modification and a site for chain lengthening. Biochemistry, 36, 8349, 1997. 

Method of enzyme modification. The method of preparation of the organic solvent-soluble enzyme called modified lipase (J) is presented below ... 

The following factors appear to control the emulsification properties of milk proteins in food product applications 1) the physico-chemical state of the proteins as influenced by pH, Ca and other polyvalent ions, denaturation, aggregation, enzyme modification, and conditions used to produce the emulsion 2) composition and processing conditions with respect to lipid-protein ratio, chemical emulsifiers, physical state of the fat phase, ionic activities, pH, and viscosity of the dispersion phase surrounding the fat globules and 3) the sequence and process for incorporating the respective components of the emulsion and for forming the emulsion. 

We have chosen to discuss enzyme modification of proteins in terms of changes in various functional properties. Another approach might have been to consider specific substrates for protease action such as meat and milk, legumes and cereals, and the novel sources of food protein such as leaves and microorganisms ( ). Alternatively, the proteases themselves provide categories for discussion, among which are their source (animals, plants, microorganisms), their type (serine-, sulfhydryl-, and metalloenzymes), and their specificity (endo- and exopeptidases, aromatic, aliphatic, or basic residue bond specificity). See Yamamoto (2) for a review of proteolytic enzymes important to functionality. 

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