Bikash Ranjan Pati

Studies on the extracellular tannase from newly isolated Bacillus licheniformis KBR 6

A tannase producing bacterial strain KBR 6 has been isolated from lateritic soil and identified as Bacillus licheniformis. It is capable of producing tannase in the medium containing only tannic acid. The rapid degradation of tannic acid and production of extracellular tannase was observed in three different media containing tannic acid (M1), tannic acid + basal salt (M2) and tannic acid + basal salt + glucose (M3). Maximum enzyme production and growth of the organism was obtained at 18–21 h and 30–36 h, respectively. The increased order of enzyme production in relation to different media is as per the following sequence, M3 > M2 > M1. The maximum growth and enzyme production was observed at pH 5.0. The pH and temperature optima of the enzyme activity were found to be at 5.75 and 60 °C respectively. Paper chromatographic analysis indicates that gallic acid is the enzymatic degradative product of tannic acid.

Production of tannase by the immobilized cells of Bacillus licheniformis KBR6 in Ca-alginate beads

Aims:  The present study was aimed at finding the optimal conditions for immobilization of Bacillus licheniformis KBR6 cells in calcium‐alginate (Ca‐alginate) beads and determining the operational stability during the production of tannin‐acyl‐hydrolase (tannase) under semicontinous cultivation.

Production of cellulase-free xylanase by Trichoderma reesei SAF3

A xylanase producing fungi has been isolated from soil and identified as Trichoderma reesei SAF3. Maximum growth of the organism was found at 48 h under submerged condition in xylan containing enriched medium, whereas highest enzyme production (4.75U/mL) was recorded at 72 h. No detectable cellulase activity was noted during whole cultivation period. The partially purified enzyme hydrolyzed xylan into xylopentose and xylose. All these properties of xylanase highlighten its promising uses in industrial scale.

Biosynthesis, structural architecture and biotechnological potential of bacterial tannase: A molecular advancement

Tannin-rich materials are abundantly generated as wastes from several agroindustrial activities. Therefore, tannase is an interesting hydrolase, for bioconversion of tannin-rich materials into value added products by catalyzing the hydrolysis of ester and depside bonds and unlocked a new prospect in different industrial sectors like food, beverages, pharmaceuticals, etc. Microorganisms, particularly bacteria are one of the major sources of tannase. In the last decade, cloning and heterologous expression of novel tannase genes and structural study has gained momentum. In this article, we have emphasized critically on bacterial tannase that have gained worldwide research interest for their diverse properties. The present paper delineate the developments that have taken place in understanding the role of tannase action, microbial sources, various cultivation aspects, downstream processing, salient biochemical properties, structure and active sites, immobilization, efforts in cloning and overexpression and with special emphasis on recent molecular and biotechnological achievements.

Fungal endophytes in three medicinal plants of Lamiaceae.

Three medicinal plants Ocimum sanctum, Ocimum bacilicum and Leucas aspera were screened to study endophytic diversity of the plants. Altogether 103 fungal endophytes belonging to fourteen genera were isolated. Leaves of all three medicinal plants were colonized by a great number of endophytic fungi. Leaves of O. sanctum were colonized by the most, that is, eleven endophytes. Highest Shannon-Wiener index (2.256) was exhibited by O. sanctum with the highest Simpsons diversity (0.8654) indicating great species specificity. O. bacilicum and L. aspera showed the highest similarity coefficient. Some fungal genera have been showed to be host specific. In the present study Curvularia sp., Hymenula sp., Tricoderma sp. and Tubercularia sp. exclusively colonized O. sanctum ; whereas Alternaria sp. and Spicaria sp. colonized only L. aspera .

Antimicrobial activity of the leaf extracts of Hyptis suaveolens (L.) poit

Steam distillation, petroleum ether, and ethanol extracts from Hyptis suaveolens leaves were evaluated for their antimicrobial activity in vitro . Steam distillation extract exhibited broad-spectrum antibacterial and antifungal activity against the tested organisms. It showed highest antifungal and antibacterial activity against Aspergillus niger and Micrococcus luteus, respectively. Activity indices of A. niger against miconazole (25 µg/ml) and M. luteus against chloramphenicol (10 µg/ml) were 0.89 and 0.67, respectively.

Tannase Production by Penicillium purpurogenum PAF6 in Solid State Fermentation of Tannin-Rich Plant Residues Following OVAT and RSM

Tannase production by newly isolated Penicillium purpurogenum PAF6 was investigated by ‘one variable at a time’ (OVAT) approach followed by response surface methodology (RSM). Tannin-rich plant residues were used as supporting solid substrate and sole carbon source and, among them, tamarind seed was found to be the most favorable substrate than haritaki, pomegranate, tea leaf waste and arjun fruit. Physicochemical parameters were initially optimized using OVAT methodology and some important factors like incubation time, incubation temperature, substrate:moisture ratio as well as carbon, nitrogen and phosphate concentrations were verified with Box–Behken design of response surface methodology. Phosphate source, nitrogen source and temperature were found as the most favorable variables in the maximization of production. Tannase production was enhanced from 1.536 U/g to 5.784 U/g using tamarind seed OVAT optimization and further enhancement up to 6.15 U/g following RSM. An overall 3.76- and 4.0-fold increases in tannase production were achieved in OVAT and RSM, respectively.

Purification and characterization of an endoxylanase from the culture broth of Bacillus cereus BSA1

An extracellular xylanase from the fermented broth of Bacillus cereus BSA1 was purified and characterized. The enzyme was purified to 3.43 fold through ammonium sulphate precipitation, DEAE cellulose chromatography and followed by gel filtration through Sephadex-G-100 column. The molecular mass of the purified xylanse was about 33 kDa. The enzyme was an endoxylanase as it initially degraded xylan to xylooligomers. The purified enzyme showed optimum activity at 55°C and at pH 7.0 and remained reasonably stable in a wide range of pH (5.0–8.0) and temperature (40–65°C). The Km and Vmax values were found to be 8.2 mg/ml and 181.8 μmol/(min mg), respectively. The enzyme had no apparent requirement of cofactors, and its activity was strongly inhibited by Cu2+, Hg2+. It was also a salt tolerant enzyme and stable upto 2.5 M of NaCl and retained its 85% activity at 3.0 M. For stability and substrate binding, the enzyme needed hydrophobic interaction that revealed when most surfactants inhibited xylanase activity. Since the enzyme was active over wide range of pH, temperature and remained active in higher salt concentration, it could find potential uses in biobleaching process in paper industries.

Novel route of tannic acid biotransformation and their effect on major biopolymer synthesis in Azotobacter sp. SSB81.

To examine tannic acid (TA) utilization capacity by nitrogen‐fixing bacteria, Azotobacter sp. SSB81, and identify the intermediate products during biotransformation. Another aim of this work is to investigate the effects of TA on major biopolymers like extracellular polysaccharide (EPS) and polyhydroxybutyrate (PHB) synthesis.

Detection of trivalent arsenic [As(III)] complex with DNA: A spectroscopic investigation

Arsenite [As(III)] is well known to exert mutagenic or carcinogenic effects. Arsenic (III) binds proteins with its cystine–SH group to DNA. Overall binding constant K = 1.12 × 104 M−1 and exponential decay constant T 1 = 271 s for DNA–As (III) interaction were measured spectrophometrically at λ max = 260 nm. Fourier transform infrared (FTIR) spectrometric method was used to charac-terize and determine the arsenite binding site in DNA–As(III) interaction. FTIR spectroscopic results showed that As(III) indirectly binds to the nitrogen bases of DNA and predominantly affected the H-bonded OH and NH bands, whereas no interaction was found with phosphate groups. No transitions from B to A or B to Z was observed in B-DNA structure.