Degradation, amylase

Some of the enzymes discussed above have been detected in filtered water samples free of particulate matter. These include the phosphatases and the starch-degrading amylases. Generally, free enzymes appear to be more abundant in sediments than in the water column (Kim and Zobell, 1972), but at times some of them, such as alkaline phosphatase, can be as active as their particle-bound forms (Berman, 1970). Dissolved extracellular enzymes are presumably excreted by various microorganisms, or perhaps are released during cell degradation or lysis. 

Of particular importance for modifications of starch are the enzyme degradation products such as glucose symps, cyclodextrins, maltodextrins, and high fmctose com symps (HFCS). Production of such hydrolysis products requites use of selected starch-degrading enzymes such as a-amylase,... 

P-amylase, and debranching enzymes. Conversion of D-glucose to D-fmctose is mediated by glucose isomerase, mosdy in its immobilized form in columns. Enzymic degradation of starch to symps has been well reviewed (116—118), and enzymic isomerization, especially by immobilized glucose isomerase, has been fiiUy described (119) (see Syrups). 

A single hydrolase is usually inadequate for the degradation of a carrier, but most hydrolases have unspecific activities, i.e., they split the chains of polymers that are not their typical substrates. For example, chitosan is susceptible to lipases, pectinases, amylases among others [257-260]. 

The only example of this technique applied to the amylose component is that already described, of the action of Z-enzyme on the /3-limit dextrin. In the case of amylopectin, enzymic methods enable a distinction to be made between the proposed laminated and highly ramified structures (I and III, in Fig. 1, page 352). The method used by Peat and coworkers101 involves the successive action of /3-amylase and R-enzyme on waxy maize starch. /3-Amylolysis will degrade A-chains down to two or three units from the 6 —> 1-a-D interchain linkages. These latter linkages will protect the... 

K. H. Meyer s scientific life took a new direction when a large segment of his laboratory was devoted to the study of the degradative enzymes of starch, the amylases. With the cooperation of Bernfeld first, then of E. H. 

In this chapter we describe the use of pea seeds to express the bacterial enzyme a-amylase. Bacterial exoenzymes like the heat stable a-amylase from Bacillus licheni-formis are important for starch hydrolysis in the food industry. The enzymatic properties of a-amylase are well understood [13,14], it is one of the most thermostable enzymes in nature and it is the most commonly used enzyme in biotechnological processes. Although fermentation in bacteria allows highly efficient enzyme production, plant-based synthesis allows in situ enzymatic activity to degrade endogenous reserve starch, as shown in experiments with non-crop plants performed under greenhouse conditions [12,15]. Finally, the quantitative and sensitive detection of a-amylase activ-... 

Malto-oligosaccharide aldonolactones react with ethylenediamine to give Ar-(2-aminoethyl)aldonamides (113-115), which have been successfully grafted onto carriers via amide linkages. The malto-oligosaccharides were produced by degradation of amylose with alpha amylase. After purification of the oligosaccharides, they were converted into the lactones by hypoiodite or electrolytic oxidation. 

For the reasons stated above, deep intrusion of degrading microbes into polysaccharide-plastic films is demonstrably and theoretically improbable. Since starch removal does occur when the films are buried in soil, the primary mechanism must be microbial production of amylase in or near a pore, diffusion of the enzyme into pores and diffusion of soluble digestion products back to the surface where they are metabolized (Figure 3). This mechanism would be the only choice when the pore diameter is too small to admit a microbial cell (i.e., at diameters < 0.5 /im). An alternative mechanism could be diffusion of a water-soluble polysaccharide to the film surface, at which point degradation would occur. None of the materials used in these investigations showed loss of starch even when soaked in water for extended periods with microbial inhibitors present. Therefore, diffusion of amylase to the substrate rather than diffusion of the substrate to the film surface is the more likely mechanism. 

The scheme proposed above requires microbial colonization of the material and excludes degradation by amylases and cellulases that are present in soils (28), but are not newly synthesized or associated with microbial cells. Active polysaccharide hydrolases are found in nearly all soils, but these enzymes are primarily bound to soil organic matter or mineral components attachment is firm enough to severely limit migration of the enzymes from surrounding soil to the film. 

Decay will not occur if the dimensions of the degradable component are so small that neither microbial intrusion nor amylase diffusion into the material can take place. 

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