Enzymes functional properties

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. 

The leaves of Camellia sinensis are similar to most plants in general morphology and contain all the standard enzymes and stmctures associated with plant cell growth and photosynthesis (10—12). Unique to tea plants are large quantities of flavonoids and methylxanthines, compounds which impart the unique flavor and functional properties of tea. The general composition of fresh tea leaves is presented ia Table 1. 

Proteins are the indispensable agents of biological function, and amino acids are the building blocks of proteins. The stunning diversity of the thousands of proteins found in nature arises from the intrinsic properties of only 20 commonly occurring amino acids. These features include (1) the capacity to polymerize, (2) novel acid-base properties, (3) varied structure and chemical functionality in the amino acid side chains, and (4) chirality. This chapter describes each of these properties, laying a foundation for discussions of protein structure (Chapters 5 and 6), enzyme function (Chapters 14-16), and many other subjects in later chapters. 

The introduction of redox activity through a Co11 center in place of redox-inactive Zn11 can be revealing. Carboxypeptidase B (another Zn enzyme) and its Co-substituted derivative were oxidized by the active-site-selective m-chloroperbenzoic acid.1209 In the Co-substituted oxidized (Co111) enzyme there was a decrease in both the peptidase and the esterase activities, whereas in the zinc enzyme only the peptidase activity decreased. Oxidation of the native enzyme resulted in modification of a methionine residue instead. These studies indicate that the two metal ions impose different structural and functional properties on the active site, leading to differing reactivities of specific amino acid residues. Replacement of zinc(II) in the methyltransferase enzyme MT2-A by cobalt(II) yields an enzyme with enhanced activity, where spectroscopy also indicates coordination by two thiolates and two histidines, supported by EXAFS analysis of the zinc coordination sphere.1210... 

DNA polymerases from several different animal cells have been isolated and studied. The three DNA polymerases of animal cells, called a, p, and y, can be distinguished by their molecular weights, template specificity, and sensitivity to sulfhydryl reagents. Table 14.3 compares the three in regard to these differences. DNA polymerase a is probably the most important for DNA replication. This enzyme shares many functional properties with DNA polymerase III of E. coli ... 

Lactamases have been classified according to either molecular characteristics or according to their functional properties. Using amino acid sequencing, Ambler [19] categorized these enzymes into four molecular classes, desig-... 

Compositional differences in the pea seeds influence the quality of the end products. Pea flours have been used for protein enrichment of a number of cereal-based products however, undesirable sensory characteristics may limit their use, in spite of improved functional effects in food systems. The production of volatile compounds during cooking and baking of foods with pea supplementation affects their acceptability. Enzyme systems active in unheated pea flours may contribute to their functional properties, but adversely affect the sensory quality of the food. 

While nature uses coenzyme-dependent enzymes to influence the inherent reactivity of the coenzyme, in principle, any chemical microenvironment could modulate the chemical properties of coenzymes to achieve novel functional properties. In some cases even simple changes in solvent, pH, and ionic strength can alter the coenzyme reactivity. Early attempts to present coenzymes with a more complex chemical environment focused on incorporating coenzymes into small molecule scaffolds or synthetic host molecules such as cyclophanes and cyclo-dextrins [1,2]. While some notable successes have been reported, these strategies have been less successful for constructing more complex coenzyme microenvironments and have suffered from difficulties in readily manipulating the structure of the coenzyme microenvironment. 

The producers of the multi-nutrient complex Grinization use low-temperature non-enzyme processing of the input product. The partial hydrolysis of nucleoproteins, lipoproteins and proteins occurs. This allows the compounds to be obtained in the globular state whereby their functional properties are preserved but with the loss of tissue specificity. Due to the use of such a technology, all the nutrients enter the human organism in bioaccessible forms. 

In vitro, the enzyme is able to catalyze crosslinking of whey proteins, soy proteins, wheat proteins, beef myosin, casein, and crude actomyosin (which is refined from mechanically deboned meat), improving functional properties such as the texture of food products [49-53], Bonds formed by transglutaminase exhibit a high resistance to proteolytic degradation [54],... 

In this section, enzymes in the EC 2.4. class are presented that catalyze valuable and interesting reactions in the field of polymer chemistry. The Enzyme Commission (EC) classification scheme organizes enzymes according to their biochemical function in living systems. Enzymes can, however, also catalyze the reverse reaction, which is very often used in biocatalytic synthesis. Therefore, newer classification systems were developed based on the three-dimensional structure and function of the enzyme, the property of the enzyme, the biotransformation the enzyme catalyzes etc. [88-93]. The Carbohydrate-Active enZYmes Database (CAZy), which is currently the best database/classification system for carbohydrate-active enzymes uses an amino-acid-sequence-based classification and would classify some of the enzymes presented in the following as hydrolases rather than transferases (e.g. branching enzyme, sucrases, and amylomaltase) [91]. Nevertheless, we present these enzymes here because they are transferases according to the EC classification. 

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