Proteins isolated from extremophiles have found application in multiple industri
ID: 508715 • Letter: P
Question
Proteins isolated from extremophiles have found application in multiple industries due to their ability to retain activity under extreme conditions. Proteins from extremophiles also serve as model system to study the relationships between protein stability, structure, and function. Lessons learned from these proteins could provide us with the information necessary to engineer new proteins from mesophilic organisms with desirable characteristics. Many detergents on the market today contain proteins (enzymes such as proteases, lipases, amylases, and cellulases) to help remove stains that have a biological origin, such as those from food and blood. Estimates put the detergent enzyme market at more than $1 billion. By what means would washing conditions induce activity loss in proteins added to detergents? Given your answer to question 7, What characteristics would be desirable in proteins that are used in the detergent industry? How might you engineer a protein that would be suitable for inclusion in a laundry detergent (the protein must retain its activity under washing conditions).Explanation / Answer
Some enzymes because of there catalytic properties to break down other proteins, fats are used in laundry detergents to break down stains of blood, eggs, food. An enzyme can break down certain specific compounds.
Protease help to break down proteins, fats
Amylase - carbohydrates
7. Washing conditions like high temperatures 40 to 60 or more than 100 degrees. An altered PH less than 8, stable to ionic , oxidation reactions or functional groups, other ionic changes with Surfactants and bleaches.
8. Stable at alkaline PH between 8 to 10. Stable at high temperatures more than 100 degreed. Should not undergo oxidation, ionic reactions with bleaches, perfumed chemicals etc. Specificity to hydrolytic break down peptide bonds.
9.Protein engineering is more evolved now to produce , enhance enzyme proteins stability and retain properties.
It involves amino group modification of active site in enzyme. By replacing this oxidative functional group with non oxidable ( by treating with H2O2) better stability can be achieved.
Deamidation of certain asparagine containing protein enzymes subtilisin can enhance PH related stability and also thermostability.
Disulfide bond bridge created artificially in the enzymes can also enhance stability.
Preparing certain mutations of enzyme proteins which have organic solvent solubility.
Charge on enzyme surface and charge -charge interactions can alter PH. cations like Ca2- binded to particular enzyme surface can enhance alkaline PH and overall activity.
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