Peptidoglycan, a major glycoconjugate in the mycobacterial cell envelope provides strength to resist osmotic stress and plays a pivotal role in maintaining the cellular morphology. Several unique growth stage specific structural alterations occur in its constituent monosaccharides and peptides that allow Mycobacterium to survive nutrient starvation and environmental stress. Here, we discuss the enzymes involved in its intricate biosynthesis that are novel targets for therapeutic intervention and provide an opportunity for potential antibiotic adjuvants. We also revisit the enzymatic steps which are critical for maintaining the equilibrium between peptidoglycan synthesis and hydrolysis during cellular growth and division specifically focused on the importance of cell wall remodelling during "exit from dormancy" in Mycobacterium, a phenomenon with tremendous physiological and therapeutic importance for intervention in mycobacterial infections.

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From various natural sources on skim milk agar plates 51protease producer bacteria wereisolated by primary screening. Secondary screening was done by zone of clearanceformed by cell free broth on gelatin agar plates. From diameter of zone of clearance potent protease best protease producers Vibrio metschnikovii strain Xmb 057 was isolated. It was biochemically characterized by performing some common biochemical tests. Effect of temperature and pH on protease by Vibrio metschnikovii strain Xmb 057 was studied. Optimum temperature and pH was 500C and 9 respectively make it suitable to be used in leather and detergent industry. Protease was tolerant to Ca++ and Mg++ which suggest its activity in detergents used even in hard water.