GC-MS Analysis, Antioxidant and Antifungal Studies of Different Extracts of Isolated from .

To discover new natural resources with biological effects, the chemical investigation of antioxidant and antimicrobial activities of extract's isolated from roots of . Gas chromatography-mass spectrometry (GC-MS) analysis demonstrated the presence of the major chemical constituents present in the methanol extract (1,3-oxathiolane, 1,3-cyclopentadiene, 5-(1-methylethylidene), 5,9-hexadecadienoic acid, methyl ester, decane), chloroform extract (acetic acid, diethoxy-, ethyl ester, 2,2-bis(ethylsulfonyl)propane, 3-methyl-2-(2-oxopropyl) furan), and hexane extract (3-hexanone, 4,4-dimethyl, decane,2,6-dimethyldecane, decane, 2,4,6-trimethyl, decane, 2,4,6-trimethyl, 1-butanesulfinamide, 1,1,2,2,3,3,4,4,4-nonafluoro-N-methyl, decane). The total compound identified (56.

Nanocarriers-based immobilization of enzymes for industrial application.

Nanocarriers-based immobilization strategies are a novel concept in the enhancement of enzyme stability, shelf life and efficiency. A wide range of natural and artificial supports have been assessed for their efficacy in enzyme immobilization. Nanomaterials epitomize unique and fascinating matrices for enzyme immobilization.

Nitrile hydratase mediated green synthesis of lactamide by immobilizing Rhodococcus pyridinivorans NIT-36 cells on N, N'-Methylene bis-acrylamide activated chitosan.

In this paper green synthesis of an important commodity chemical lactamide has been undertaken using chitosan immobilized Rhodococcus pyridinivorans NIT-36 harbouring nitrile hydratase (NHase) enzyme. The cells immobilization (300 mg/g) is based on the partial entrapment of cells by suspension cross-linking technique facilitated by N, N'-Methylene bis-acrylamide. In the repeated-use experiments, the immobilized cells retained 80% of its initial activity when stored at 4 °C for 30 days.

Random Mutagenesis of Thermophilic Xylanase for Enhanced Stability and Efficiency Validated through Molecular Docking.

Background: Xylanases of thermophilic origin are more robust and stable and hence more suitable for industrial applications. The aim of the research was to develop a patent using a robust mutant exhibiting enhanced xylanase activity. The strain (Bacillus aestuarii SC-2014) subjected to mutagenesis is thermophilic in origin and hence it is envisioned that the enhancement of its catalytic potential will enhance its industrial applicability.

Purification and characterization of thermostable superoxide dismutase from Anoxybacillus gonensis KA 55 MTCC 12684.

A thermostable superoxide dismutase from thermophilic bacterium Anoxybacillus gonensis KA 55 MTCC 12684 which was isolated from Manikaran hotspring of Himachal Pradesh was purified to apparent homogeneity by fractional ammonium sulphate precipitation and anion exchange chromatography. A purification factor of 33.1-fold was achieved, with the purified enzyme exhibiting specific activity of 5758.

Restriction enzyme-mediated insertional mutagenesis: an efficient method of Rosellinia necatrix transformation.

Rosellinia necatrix: causing root rot disease is a very destructive pathogen of woody plants and is responsible for yield losses to a large number of fruit trees. The genetic analysis of this pathogen has not been picked up because of difficulty in generating mutations in Rosellinia necatrix for many reasons. A number of methods have been proposed for inducing mutations in Rosellinia necatrix but none of them proved worth because of very low transformation efficiencies.

Improving stability and reusability of Rhodococcus pyridinivorans NIT-36 nitrilase by whole cell immobilization using chitosan.

Immobilized enzymes have great significance for industrial processes. In this study whole cell immobilization of Rhodococcus pyridinivorans NIT-36 has been undertaken using chitosan microspheres as an immobilized matrix. R.