Fifty one isolates of cellulolytic bacteria were isolated from cow dung and two soil samples were obtained from Kambalakonda Wildlife Sanctuary and RCD Biodiversity Park in Visakhapatnam, Andhra Pradesh by Enrichment method in basal salt medium with cellulose as substrate for degradation. The cellulolytic activity of the isolated bacteria was determined by the diameter of the zone of hydrolysis by Gram's iodine dye staining method. After primary screening, a total of fifty one isolates showed cellulolytic activity. Out of fifty one strains of cellulolytic bacteria, twenty three isolates from Kambalakonda Wildlife Sanctuary, seventeen isolates from RCD Biodiversity Park and Eleven isolates from cow dung sample obtained from cattle ranch, Visakhapatnam showed cellulase activity. Seven strains showed maximum hydrolytic value greater than 4.0 cm, nineteen strains showed average hydrolytic value between 3.0 and 3.9 cm and twenty one strains showed minimum hydrolytic value between 1.5 and2.9 cm. The potential isolates were obtained from Kambalakonda Wildlife Sanctuary and RCD Biodiversity Park than cow dung sample. The 13 C strain exhibited maximum hydrolytic value of 5.6 cm which was designated as KKV1. The strain KKVI was identified as Streptomyces corchorusii (MN244066) by morphological, cultural, biochemical and 16S rRNA sequence. The CMCase and FPase activity of the crude sample were examined by DNS method and found to be 0.21 U/ml and 0.041 U/ml respectively and the specific activity was 4.38 U/mg proteins and 0.86 U/mg proteins respectively. The present study emphasizes that the Streptomyces corchorusii have a higher cellulase activity and the soils of bio reserves have a lot of scope for isolating high cellulolytic bacteria which can be exploited for different industrial purposes.

Objective:The objective of the present study was to characterize the monoheaded trypsin inhibitors, Abelmoschus moschatus trypsin inhibitor-I (AMTI-I) and AMTI-II from the seeds of A. moschatus with respect to their specificity, mode of action, and active site residues.Methods: Standard methods were followed in determining inhibitory activities of monoheaded inhibitors. IC 50 values and inhibitory constants (Ki) of AMTI-I and AMTI-II were determined. Studies on complex formation and chemical modification of inhibitors were performed.Results: AMTI-I and AMTI-II were found to be serpins, strongly active against trypsin, moderately active against porcine elastase, Staphylococcus aureus protease, and Aspergillus oryzae protease. AMTI-I and AMTI-II have shown non-competitive type of inhibition toward bovine trypsin with K i values of inhibitors for trypsin found to be 0.25±0.02 nM and 0.22±0.06 nM, respectively. Complex studies revealed the formation of stable 1:1 complex of trypsin with both AMTI-I and AMTI-II. Chemical modification of the functional groups of the inhibitors by selective reagents indicated that arginine residues are essential for their trypsin inhibitory activities. Conclusion:Investigations on the specificity of protease inhibitors are important for understanding their physiological role, control mechanisms involved in the regulation of proteolysis in biological systems and mode of action.