Introduction
The enzyme protease is a group of enzymes whose main work is to break down peptide bonds of proteins. There are different types of proteases depending on the type of peptide bond each hydrolyses. Examples include trypsin, pepsin, fungal, protease, papain, bromelain, chymotrypsin and subtilisin (Mikel, 2004).
Industrial application of enzyme protease
alkaline proteases is largely used in the Leather industry where it dehairs hides. Sodium sulfide used to be used long before alkaline protease came into use. Its use is safer in terms of occupational health hazards. The process of dehairing hides is closely monitored in order to improve the quality of leather (Mikel, 2004).
Other uses of the enzyme protease
These include its use in the process of brewing, baking, protein processing, distilling spirits, manufacturing of washing and laundry detergents, lens cleaners and manufacture of some chemicals. The use of protease in the medical field is currently gaining momentum as more research and clinical studies have shown its benefits in the medical fields of oncology, inflammatory conditions, blood rheology control, and immune regulation. Proteases are commercially manufactured through a highly aseptic procedure for food supplementation and enzyme therapy. Aspergillus niger and oryzae are commonly used to manufacture proteases commercially (Pınar Çalík, et al 1998; Mikel, 2004).
Conclusion
Enzyme protease has several industrial importance with potential uses if more research studies can be done on its use. Its proteolytic ability can be explored to determine its undiscovered uses. One area that needs further studies is the ability of fungal protease to reduce concentrations of heavy metals such as lead in heavy metal poisoning (HMP). This will help in management of HMP (Mikel, 2004).
References
- Mikel, J. K., (2004). Enzyme protease: Industrial use. Nairobi, Kenya: Paloma Publishers.
- Pınar Çalík, et al (1998). Oxygen transfer effects in serine alkaline protease fermentation by Bacillus licheniformis: use of citric acid as the carbon source. Enzyme and microbial technology (23)7-8, 451-461