Shivaji University

About: Shivaji University is a education organization based out in Kolhāpur, Maharashtra, India. It is known for research contribution in the topics: Thin film & Scanning electron microscope. The organization has 3078 authors who have published 5295 publications receiving 115397 citations.

Identification of Water Deficit Stress Upregulated Genes in Sugarcane

Abstract: Sugarcane represents an important renewable source among biofuel crops with high capability to assimilate carbon among the C4 plants. Limited availability of freshwater renders this crop uneconomical, warranting the necessity for the development of varieties with higher water use efficiency and tolerant to water deficiency stress. Sugarcane variety cv. Co740 was subjected to varied levels of water deficiency stress to isolate transcripts differentially expressed to the imposed stress. The leaf relative water content was used as a measure to estimate the stress response. PCR-based cDNA suppression subtractive hybridization technique was applied to construct forward subtracted library for differentially expressed genes under stress. Dot blot-selected 158 clones showing elevated response were sequenced, of which 62% resembled similarity with known functional genes, 12% with hypothetical proteins of plant origin, while 26% represented new unknown sequences. Annotation of these differentially expressed sequence tags (ESTs) in the moderately water deficit stress-tolerant cultivar predicted that most of them encoded proteins involved in cellular organization, protein metabolism, signal transduction, and transcription. Further, semi-quantitative reverse transcriptase PCR carried out for five genes projected the involvement of these ESTs in stress alleviation/tolerance. Results from this study may help in targeting useful genes for improving drought tolerance in sugarcane and other grasses.

Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A

Abstract: The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o -tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40 °C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30 V. The laccase was stable up to 40 °C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5 h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.