Polymer by enzymes

FIGURE 4 Schematics for the synthesis of aromatic polymers by enzyme-catalyzed reactions. 

Aliphatic polyesters are perhaps some of the most easily biodegraded polymers found in nature. One reason for this is the effect that chain flexibility has on biodegradability. For degradation of polymers by enzymes, the polymer chain must be flexible enough to fit into the active site of the enzyme. This characteristic most likely accounts for the biodegradability of aliphatic polyesters, which are flexible, whereas wholly aromatic polyesters, which are more rigid, are generally considered bioinert. 

Currently, a-amino acids are prepared by several routes such as by the fermentation of glucose, by enzyme action on several substances and by the hydrolysis of proteins. Many methods for synthesising the polymers are known, of which the polymerisation of A -carboxyanhydrides is of particular interest, as it yield-products of high molecular weight (Figure 18.24). 

The interest in this area may be seen to stem from the biological area where the phenomenon is well known and accounts for the regularity in the structure of natural proteins and polynucleotides. Such polymers are efficiently synthesized by enzymes which arc capable of organizing monomer units within regularly structured molecular-scale spaces and exploiting weak forces such as hydrogen bonds and Van der Waal forces to control the polymerization process.. 

The complex polymers in feedstuffs are broken down to the constituent building blocks by a sequential process. Hydrolysis of the polymers is initiated in the lumen of the GIT by enzymes and other secretions produced by the pancreas, stomach, intestine, liver and gall bladder, and other GIT tissues, and completed by another suite of enzymes associated with the brush border membrane (BBM) or intracellular organelles. Anti-nutrient phytochemicals can decrease the hydrolysis of feedstuffs, and thereby reduce nutrient availability, either by increasing the inherent resistance of the polymers to hydrolysis or by decreasing the activities or amounts of enzymes and other secretions produced by the GIT. 

Enzymes are generally classified into six groups. Table 1 shows typical polymers produced with catalysis by respective enzymes. The target macromolecules for the enzymatic polymerization have been polysaccharides, poly(amino acid)s, polyesters, polycarbonates, phenolic polymers, poly(aniline)s, vinyl polymers, etc. In the standpoint of potential industrial applications, this chapter deals with recent topics on enzymatic synthesis of polyesters and phenolic polymers by using enzymes as catalyst. 

Poly-j3-malate is readily degraded completely to L-malic acid under both acid and base conditions [108], and it can also be hydrolyzed by enzymes within the cell [105,106]. Recently, several bacteria were isolated which were able to utilize poly-/i-malate as sole carbon source for growth [109]. Because the polymer is biodegradable and bioadsorbable, it is of considerable interest for pharmaceutical applications, especially in controlled-release drug delivery systems [97,98]. Chemical routes to poly-/ -malate are expected to provide materials with various properties [110]. 

Production of all naturally occurring polymers in vivo is catalyzed by enzymes. Polymerizations catalyzed by an enzyme ( enzymatic polymerizations ) have received much attention as new methodology [6-11], since in recent years structural variation of synthetic targets on polymers has begun to develop highly selective polymerizations for the increasing demands in the production of various functional polymers in material science. So far, in vitro syntheses of not only biopolymers but also non-natural synthetic polymers through enzymatic catalysis have been achieved [6-11]. 

Since many proteases are specific in cleaving peptide linkages adjacent to substituent groups, we decided to prepare substituted polymers, anticipating that the introduction of the substituents would make the polymers more degradable. Methylated, benzylated, and hydroxylated polymers were prepared and their biodegradations have been studied. Compared to the unsubstituted polymers we found the substituted polymers more susceptible to attack by enzymes and microorganisms. (4, 6)... 

A novel concept of using bioadhesive polymers as enzyme inhibitors has been developed [97]. Included are derivatives of poly acrylic acid, polycarbophil, and car-bomer to protect therapeutically important proteins and peptides from proteolytic activity of enzymes, endopeptidases (trypsin and a-chymotrypsin), exopeptidases (carboxypeptidases A and B), and microsomal and cytosolic leucine aminopeptidase. However, cysteine protease (pyroglutamyl aminopeptidase) is not inhibited by polycarbophil and carbomer [97]. 

Realini and Althaus [313] have put forth the hypothesis that poly(ADP-ribosylation) may have a function in histone shuttling. They propose that poly(ADP-ribose) polymerase directed to sites of DNA strand breaks would auto-modify itself generating multiple ADP-ribose polymers. The polymers would lead to the dissociation of the histones from DNA onto the polymers. The DNA would now be free for processing (e.g., by enzymes involved in excision repair). The action of poly(ADP-ribose) glycohydrolase would degrade the... 

Synergism between a-arabinosidase, xylanase and j8-xylosidase has been demonstrated in the hydrolysis of wheat straw arabinoxylan with purified enzymes of T, reesei (71). > en only xylanase and )8-xylosidase were used in the hydrolysis, the xylose yield was only 66% of that produced by the whole culture filtrate at the same activity levels of these two enzymes, and no arabinose was produced. Addition of a-arabinosidase increased the yields of both xylose and arabinose. Enhanced hydrolytic action of hemicellulolytic or pectinolytic enzymes in the hydrolysis of alfalfa cell wall polymers by addition of Ruminococcus albus a-arabinosidase has also been reported (37). 

In this paper we have immobilized an enzyme within a thermally reversible hydrogel. Immobilized enzymes have been used in a variety of applications, ranging from treatment of diseases to sensors, assays, and industrial processes (15-20). When an enzyme is immobilized within a gel which exhibits reversible shrinking and swelling as the ten rature is raised and lowered through the LCST of the gel matrix polymer, the enzyme may be switched off and on as the substrate diffusion rate is regulated by the gel pore size (5). In adcfition to enzymes, a variety... 

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