ABSTRACT
Aim: The present study was undertaken to establish the potential role of Achyranthes aspera Linn for cure of skin diseases. Study Design: The plant is traditionally used by various tribes for curing a wide range of diseases. A 50% ethanolic extract of the leaves was subjected to phytochemical studies and further investigated for in vitro antioxidant and antibacterial activities. Place and Duration of Study: CSIR-National Botanical Research Institute (NBRI), Lucknow, between December 2012 and November 2013. Methodology: In vitro antioxidant activity was determined by DPPH free radical scavenging assay, hydroxyl radical scavenging activity, β-Carotene-linoleic acid assay and reducing power assay. Antibacterial activity was studied by agar well diffusion method. Results: The total phenol and flavonoid content was estimated to be 3.363% and 6.36% respectively. The HPTLC analysis showed the presence of oleanolic acid, lupeol and β- sitosterol. The free radical scavenging activity of the extract was concentration dependent and IC50 was observed at a concentration of 62.24μg/ml for DPPH free radical scavenging activity and 68.32μg/ml for hydroxyl radical scavenging activity. The extract showed significant total antioxidant activity and reducing power. Antibacterial activity was studied by well diffusion method and the MIC was recorded at 0.75 mg/ml for S. aureus, 0.8 mg/ml for M. luteus, 2.75 mg/ml for E. coli and 0.8 mg/ml for P. aeruginosa. Conclusion: The results obtained from current study demonstrate that the leaf extract of Achyranthes aspera L possess significant antioxidant and antibacterial properties. Presence of various classes of phytocompounds e.g. Phenols, flavonoids, saponins, alkaloids etc. contribute highly to its medicinal values, thus indicating its potential for cure of skin diseases.
ABSTRACT
Mango peel, a solid mango processing waste, comprises 15-20% of total fruit weight. This, being a rich source of lignocelluloses, was used as substrate for carboxymethyl cellulase (CMCase) production using Paenibacillus polymyxa. Maximum CMCase production (7.814 U mg-1) was observed in a medium containing 7% mango peel (w/v) with 1.5% ammonium sulphate (w/v) at 37oC and pH 5.5. Purification to an extent of 28.24 fold was achieved by affinity column chromatography. Bands corresponding to 26.5 and 34.0 kDa molecular sizes were observed on 12% denaturing Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) while of 72 kDa on 10% non- denaturing Native-PAGE, proving its heteromeric multienzyme nature. The enzyme was stable over a range of 20-60oC and pH of 4.0-7.5. Michaelis-Menten equation constant (Km and Vmax) values of purified CMCase were 8.73 mg ml-1 and 17.805 mM ml-1 min-1, respectively.
ABSTRACT
The cells of Synechocystis sp. PCC 6803 were subjected under photoinhibitory irradiation (600 micromolm(-2)s(-1)) at various temperatures (20-40 degrees C) to study in vivo quality control of photosystem II (PSII). The protease biogenesis and its consequences on photosynthetic efficiency (chlorophyll fluorescence ratio Fv/Fm) of the PSII, D1 degradation and repair were monitored during illumination and darkness. The loss in Fv/Fm value and degradation of D1 protein occurred not only under high light exposure, but also continued when the cells were subjected under dark restoration process after high light exposure. No loss in Fv/Fm value or D1 degradation occurred during recovery under growth/low light (30 micromol m(-2) s(-1)). Further, it helped the resynthesis of new D1 protein, essential to sustain quality control of PSII. In vivo triggering of D1 protein required high light exposure to switch-on the protease biosynthesis to maintain protease pool which induced temperature-dependent enzymatic proteolysis of photodamaged D1 protein during photoinhition and dark incubation. Our findings suggested the involvement and overexpression of a membrane-bound FtsH protease during high light exposure which caused degradation of D1 protein, strictly regulated by high temperature (30-40 degrees C). However, lower temperature (20 degrees C) prevented further loss of photoinhibited PSII efficiency in vivo and also retarded temperature-dependent proteolytic process of D1 degradation.