Hydrolysis enzymatic protein processing

The plastein reaction usually involves two steps hydrolysis of protein and resynthesis of peptide links. Yamashita et al. (20) found similar BV, digestibility, and weight gain for denatured soy meal and soy plastein. This same group (49,50) had described a one-step process by which amino acids may 5 enzymatically incorporated in intact protein to improve protein quality. With soy protein they applied a racemic mixture of D,L-methionine ethyl ester and were able to enzymatically incorporate L-methionine. As Schwimmer (51) has pointed out, one expects the methionine so incorporated to be highly available due to its location at the end of the polypeptide chains. 

These processes provide a complete destruction of the structure of the hair keratin by the complete hydrolysis of proteins that compose it. Hydrolysis can occur enzymatically or chemically. 

Murakami, Y. and Hirata, A. 2000. Novel process for enzymatic hydrolysis of proteins in an aqueous two-phase system for the production of peptide mixture. Prep. Biochem. Biotechnol. 30, 31-37. 

Enzymatic hydrolysis of proteins in vivo is a very important process and it is used biologically in many ways (see Table VI). Generally these reactions can be grouped as either important for protein turnover or for... 

Amino acids can be obtained by hydrolysis of proteins, chemical synthesis, fermentation (e.g. of sugars), and enzymatic processes [32], They serve similar purposes as proteins, but in addition, aspartic acid and glutamic acid were rated as top value-added chemicals, which can be converted to further fine chemicals [8]. Another example is the production of building blocks like ethylenediamine and butanediamine from serine and arginine, respectively [6],... 

Enzymatic hydrolysis of food proteins generally results in profound changes in the functional properties of the proteins treated. Protein hydrolysates may therefore be expected to fulfil certain of the food industry s demands for proteins with particular, well-defined functional properties. A wide-spread use of protein hydrolysates in food requires, however, a careful control of the taste and functionality of the protein during its hydrolysis and subsequent processing to obtain a reproducible product quality. 

Membrane processes have a potential application within many areas of industrial enzymatic hydrolysis of proteins. Table 1 shows how membrane processes can be applied in the different types of enzymatic modification of protein. Thus membrane processes may be used for pre-treatment of proteins, for the reaction step and as an essential part of the purification or posttreatment step. 

The in vivo stability of a natural polyelectrolyte complex membrane, such as is formed between alginate and polylysine, (or even between synthetic polyelectrolytes) must never be assumed due to slow site-by-site displacement reactions which may occur with high molecular weight polymers (proteins, etc.) present in body fluids, and to processes of hydrolysis, enzymatically promoted or otherwise which may disrupt the membrane. 

A Tokyo group [46] was the first to propose a combined process of enzymatic protein hydrolysis and resynthesis for producing a product with improved sensory properties and modified amino acid composition. An enzymatic reaction was used also for the removal of bound impurities [108,109], for debittering of hydrolysates [47,110], and for decolorization of proteins of particular origin [111]. 

Enzymatic phosphoryl transfer reactions are ubiquitous in nature and play significant roles in ATP hydrolysis and protein phosphorylation processess. As previously described, pentacoordinate phosphorus species have been assumed as transient intermediates or transition states in these pathways and their structural and electronic properties are undoubtedly related to the outcome of the process. Therefore, to aid understanding of the phosphorus-catalyzed biological routes, many model pentacoordinated phosphoranes have been synthesized. While most studies have focused on aspects of apicophilicity, anti-apicophilicity or Berry pseudorotation, there have been limited investigations on the stereochemistry of pentacoordinated spirophosphoranes with a chiral phosphorus atom. In the past year, much attention has been paid to the synthesis and determination of absolute configuration of several chiral pentacoordinate spirophosphoranes derived from D- and L-aminoacids. Some significant achievements in this area will be discussed in this section. 

Anandamide is inactivated in two steps, first by transport inside the cell and subsequently by intracellular enzymatic hydrolysis. The transport of anandamide inside the cell is a carrier-mediated activity, having been shown to be a saturable, time- and temperature-dependent process that involves some protein with high affinity and specificity for anandamide (Beltramo, 1997). This transport process, unlike that of classical neurotransmitters, is Na+-independent and driven only by the concentration gradient of anandamide (Piomelli, 1998). Although the anandamide transporter protein has not been cloned yet, its well characterized activity is known to be inhibited by specific transporter inhibitors. Reuptake of 2-AG is probably mediated by the same facilitating mechanism (Di Marzo, 1999a,b Piomelli, 1999). 

The absorption efficiency of the different carotenoids is variable. For example, (3-cryptoxanthin has been reported to have higher absorption efficiency than a-cryptoxanthin in rats (Breithaupt and others 2007). Carotenoids must be liberated from the food before they can be absorbed by intestinal cells (Faulks and Southon 2005). Mechanical disruption of the food by mastication, ingestion, and mixing leads to carotenoid liberation (Guyton and Hall 2001). The enzymatic and acid-mediated hydrolysis of carbohydrates, lipids, and proteins (chemical breaking of the food) also contributes to carotenoids liberation from the food matrix (Faulks and Southon 2005). Once released, carotenoids must be dissolved in oil droplets, which are emulsified with the aqueous components of the chyme. When these oil droplets are mixed with bile in the small intestine, their size is reduced, facilitating the hydrolytic processing of lipids by the pancreatic enzymes (Pasquier and others 1996 Furr and Clark 1997 ... 

The family of heterotrimeric G proteins is involved in transmembrane signaling in the nervous system, with certain exceptions. The exceptions are instances of synaptic transmission mediated via receptors that contain intrinsic enzymatic activity, such as tyrosine kinase or guanylyl cyclase, or via receptors that form ion channels (see Ch. 10). Heterotrimeric G proteins were first identified, named and characterized by Alfred Gilman, Martin Rodbell and others close to 20 years ago. They consist of three distinct subunits, a, (3 and y. These proteins couple the activation of diverse types of plasmalemma receptor to a variety of intracellular processes. In fact, most types of neurotransmitter and peptide hormone receptor, as well as many cytokine and chemokine receptors, fall into a superfamily of structurally related molecules, termed G-protein-coupled receptors. These receptors are named for the role of G proteins in mediating the varied biological effects of the receptors (see Ch. 10). Consequently, numerous effector proteins are influenced by these heterotrimeric G proteins ion channels adenylyl cyclase phosphodiesterase (PDE) phosphoinositide-specific phospholipase C (PI-PLC), which catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) and phospholipase A2 (PLA2), which catalyzes the hydrolysis of membrane phospholipids to yield arachidonic acid. In addition, these G proteins have been implicated in... 

It is noteworthy that there is another limiting factor in the choice of amino acid types at the junction sites which affect the enzymatic process of the intein. For example, in the case of SceVMA (also called PI-Seel) from the IMPACT system, proline, cysteine, asparagine, aspartic acid, and arginine cannot be at the C-terminus of the N-terminal target protein just before the intein sequence. The presence of these residues at this position would either slow down the N-S acyl shift dramatically or lead to immediate hydrolysis of the product from the N-S acyl shift [66]. The compatibility of amino acid types at the proximal sites depends on the specific inteins and needs to be carefully considered during the design of the required expression vectors. The specific amino acid requirements at a particular splicing site depends on the specific intein used and is thus a crucial point in this approach. 

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