Industrial enzymes detergent industry

FLOOD, D.F.S., BLOFELD, R.E., BRUCE, C.F., HEWITT, J.I., JUNIPER, C. P. ROBERTS, D.M. (1985) Lung function, atopy, specific hypersensitivity and smoking of workers in the enzyme detergent industry over 11 years. British Journal of Industrial... 

Bulk Enzymes. Enzymes such as proteases, amylases, glucose isomerases, and rennin are used in food processing. Similarly proteases and Hpases are used in detergents. CeUulases and xylanases are used in the paper pulp industry. The genes for most of the enzymes used in the various commercial processes have been cloned and overexpressed. Rennin (chymosin) produced from E. coli and A. nigerhas been approved by FDA for use in the dairy industry. 

Many enzymes have been the subject of protein engineering studies, including several that are important in medicine and industry, eg, lysozyme, trypsin, and cytochrome P450. SubtiHsin, a bacterial serine protease used in detergents, foods, and the manufacture of leather goods, has been particularly well studied (68). This emphasis is in part owing to the wealth of stmctural and mechanistic information that is available for this enzyme. 

The detergent industry is the largest user of industrial enzymes. The starch industry, the first significant user of enzymes, developed special symps that could not be made by means of conventional chemical hydrolysis. These were the first products made entirely by enzymatic processes. Materials such as textiles and leather can be produced in a more rational way when using enzyme technology. Eoodstuffs and components of animal feed can be produced by enzymatic processes that require less energy, less equipment, or fewer chemicals compared with traditional techniques. 

In 1958, the microbial alkaline protease Alcalase (Novo Industries) was produced by fermentation of a strain of Bacillus licheniformis. It had high StabiHty and activity at pH 8—10, was marketed in 1961, and was incorporated into Bio 40. However, it was not until the successful marketing of the presoaking agent Biotex in 1963 that detergent manufacturers saw the tme possibiHties of enzymes. 

Recovery. The principal purpose of recovery is to remove nonproteinaceous material from the enzyme preparation. Enzyme yields vary, sometimes exceeding 75%. Most industrial enzymes are secreted by a microorganism, and the first recovery step is often the removal of whole cells and other particulate matter (19) by centrifugation (20) or filtration (21). In the case of ceU-bound enzymes, the harvested cells can be used as is or dismpted by physical (eg, bead mills, high pressure homogenizer) and/or chemical (eg, solvent, detergent, lysozyme [9001 -63-2] or other lytic enzyme) techniques (22). Enzymes can be extracted from dismpted microbial cells, and ground animal (trypsin) or plant (papain) material by dilute salt solutions or aqueous two-phase systems (23). 

The growth in volume of the enzyme business from 1980 to 1990 is estimated to be 5—10% per year. The estimated worldwide enzyme sales per industry are shown in Table 7. The detergent and starch conversion industries are by far the most important, and account for 60% of total enzyme sales. Five principal industries account for around 85% of enzyme sales, whereas the remaining sales are spread over many different industries. 

Chemical lysis, or solubilization of the cell wall, is typically carried out using detergents such as Triton X-100, or the chaotropes urea, and guanidine hydrochloride. This approach does have the disadvantage that it can lead to some denaturation or degradation of the produci. While favored for laboratory cell disruption, these methods are not typically used at the larger scales. Enzymatic destruction of the cell walls is also possible, and as more economical routes to the development of appropriate enzymes are developed, this approach could find industrial application. Again, the removal of these additives is an issue. 

Proteases are hydrolytic enzymes with important application in industries, in particular, in detergent and in the food industry. A metagenomic study in which 100 000 plasmid clones were screened for proteolytic activity found one positive done, which was determined to be novel by sequencing analysis [84]. 

Archaea or Archaebacteria, which live in sulphurous waters around undersea volcanic vents. An extraordinarily stable enzyme which functions even at 135 °C and survives at pH 3.2-12.7 has been identified [142]. This enzyme has been termed STABLE (stalk-associated archaebacterial endoprotease). It is suggested that such exceptional stability may be attributable to unusually large Mr and tight folding of the protein chain. Suggested uses include washing powders and detergents, as well as industrial catalysts. It is even proposed that such remarkable properties may have contributed to the early evolution of life on earth [142]. 

Schweigert, M.K., Mackenzie, D.P., and Sarlo, K., Occupational asthma and allergy associated with the use of enzymes in the detergent industry a review of the epidemiology, toxicology and methods of prevention, Clin Exp Allergy, 30, 1511, 2000. 

Detergent enzymes, 10 273—286 cleaning effects of, 10 275 functions of, 10 274—275 performance evaluation of, 10 276—278 Detergent fragrances, 18 362 Detergent industry... 

Nicholson, P. J., Newman Taylor, A. J., Oliver, P., and Cathcart, M. (2001). Current best practice for the health surveillance of enzyme workers in the soap and detergent industry. Occup. Med. 51, 81-92. 

A practical enzymatic procedure using alcalase as biocatalyst has been developed for the synthesis of hydrophilic peptides.Alcalase is an industrial alkaline protease from Bacillus licheniformis produced by Novozymes that has been used as a detergent and for silk degumming. The major enzyme component of alcalase is the serine protease subtilisin Carlsberg, which is one of the fully characterized bacterial proteases. Alcalase has better stability and activity in polar organic solvents, such as alcohols, acetonitrile, dimethylformamide, etc., than other proteases. In addition, alcalase has wide specificity and both l- and o-amino acids that are accepted as nucleophiles at the p-1 subsite. Therefore, alcalase is a suitable biocatalyst to catalyse peptide bond formation in organic solvents under kinetic control without any racemization of the amino acids (Scheme 5.1). 

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