1.5. Enzyme-Polysaccharide Interactions
Proteins and enzymes have become an integral part of many industrial processes as well as being applied both in cosmetics and in therapeutics. Due to advances in biotechnology and genetic engineering, mass production of protein and enzymes has become feasible. Use of enzymes is environmentally friendly as they catalyse reactions under mild conditions against polluting inorganic catalysts which works in the extremes of pH and temperature. However, this can be disadvantageous as enzymes can lose their structure and catalytic activity at process conditions that might be necessary for other components. This often becomes a constraint in using them commercially. Increase in stability is therefore of great …show more content…
Some examples of high temperature enzymatic processes are:
• Conversion of glucose to high fructose syrup at 60–65ºC by glucose isomerase
• Starch hydrolysis by α-amylase (85–110ºC) and glucoamylase (55–65ºC)
• Washing with protease containing detergents at 60ºC
• Degradation of cellulose at 65–70ºC by cellulase
Two ways to obtain thermally stable enzymes are by isolation from microbial source, or by stabilizing already known enzymes. The former approach has drawbacks such as laborious and time consuming job of screening of microorganism and maintenance of the culture. However, the later approach is gaining attraction over a year to develop suitable biocatalyst from an already known …show more content…
According to excluded volume theory, crowding provides a non-specific force that promotes processes resulting in a reduction of total excluded volume. This occurs by the formation of macromolecular complexes and the adoption of compact macromolecular conformations. Molecular crowding plays a significant role in protein folding and aggregation in vivo which suggested its importance in conformational or aggregation states. This crowding does not occur in dilute solution and hence does not show any conformational benefits to protein (Ptitsyn, 1995). A study on the effect of sugars on the conformation of several unfolded proteins suggested the importance of volume exclusion effect. A protein maintains compact molten globule conformation in the presence of high concentrations of sugar (Davis-Searles et al., 1998). The presence of macromolecules near a protein could alter its folding energy landscape simply through the excluded volume effect and hence help to maintain compact polypeptide chain (Minton,
Proteins and enzymes have become an integral part of many industrial processes as well as being applied both in cosmetics and in therapeutics. Due to advances in biotechnology and genetic engineering, mass production of protein and enzymes has become feasible. Use of enzymes is environmentally friendly as they catalyse reactions under mild conditions against polluting inorganic catalysts which works in the extremes of pH and temperature. However, this can be disadvantageous as enzymes can lose their structure and catalytic activity at process conditions that might be necessary for other components. This often becomes a constraint in using them commercially. Increase in stability is therefore of great …show more content…
Some examples of high temperature enzymatic processes are:
• Conversion of glucose to high fructose syrup at 60–65ºC by glucose isomerase
• Starch hydrolysis by α-amylase (85–110ºC) and glucoamylase (55–65ºC)
• Washing with protease containing detergents at 60ºC
• Degradation of cellulose at 65–70ºC by cellulase
Two ways to obtain thermally stable enzymes are by isolation from microbial source, or by stabilizing already known enzymes. The former approach has drawbacks such as laborious and time consuming job of screening of microorganism and maintenance of the culture. However, the later approach is gaining attraction over a year to develop suitable biocatalyst from an already known …show more content…
According to excluded volume theory, crowding provides a non-specific force that promotes processes resulting in a reduction of total excluded volume. This occurs by the formation of macromolecular complexes and the adoption of compact macromolecular conformations. Molecular crowding plays a significant role in protein folding and aggregation in vivo which suggested its importance in conformational or aggregation states. This crowding does not occur in dilute solution and hence does not show any conformational benefits to protein (Ptitsyn, 1995). A study on the effect of sugars on the conformation of several unfolded proteins suggested the importance of volume exclusion effect. A protein maintains compact molten globule conformation in the presence of high concentrations of sugar (Davis-Searles et al., 1998). The presence of macromolecules near a protein could alter its folding energy landscape simply through the excluded volume effect and hence help to maintain compact polypeptide chain (Minton,