Adsorption of Lead on Lentil Husk in Fixed Bed Column Bioreactor.

This study depicts successful employment of fixed bed column bioreactor for adsorption of lead in continuous mode using lentil husk as sorbent. Design parameters considerably controlled the reactor performance, amongst which height of the fixed bed and flow rate were crucial in generating cleaner effluent. Adsorption capacity was found to shoot up to the level of 205.87 mg g-1 at 10 cm bed height, 100 mg L-1 feed concentration and 20 mL min-1 flow rate. Kinetic study done at regular intervals of time revealed high percentage removal of lead (99-96%) throughout entire span of reactor operation. Experimental data were well interpreted by Thomas model and Yoon-Nelson model. The reactor bed was regenerated after each adsorption and loaded metal was recovered up to the extent of ∼96%. The column reactor was efficient enough to treat lead containing actual industrial effluents.

Enzymes- An Existing and Promising Tool of Food Processing Industry.

BACKGROUND: The enzyme catalyzed process technology has enormous potential in the food sectors as indicated by the recent patents studies. It is very well realized that the adaptation of the enzyme catalyzed process depends on the availability of enzyme in affordable prices. OBJECTIVE: Enzymes may be used in different food sectors like dairy, fruits & vegetable processing, meat tenderization, fish processing, brewery and wine making, starch processing and many other. Commercially only a small number of enzymes are used because of several factors including instability of enzymes during processing and high cost. METHOD: More and more enzymes for food technology are now derived from specially selected or genetically modified microorganisms grown in industrial scale fermenters. Enzymes with microbial source have commercial advantages of using microbial fermentation rather than animal and plant extraction to produce food enzymes. CONCLUSION: At present only a relatively small number of enzymes are used commercially in food processing. But the number is increasing day by day and field of application will be expanded more and more in near future. The purpose of this review is to describe the practical applications of enzymes in the field of food processing.

Performance study of chromium (VI) removal in presence of phenol in a continuous packed bed reactor by Escherichia coli isolated from East Calcutta Wetlands.

Organic pollutants, like phenol, along with heavy metals, like chromium, are present in various industrial effluents that pose serious health hazard to humans. The present study looked at removal of chromium (VI) in presence of phenol in a counter-current continuous packed bed reactor packed with E. coli cells immobilized on clay chips. The cells removed 85% of 500 mg/L of chromium (VI) from MS media containing glucose. Glucose was then replaced by 500 mg/L phenol. Temperature and pH of the MS media prior to addition of phenol were 30°C and 7, respectively. Hydraulic retention times of phenol- and chromium (VI)-containing synthetic media and air flow rates were varied to study the removal efficiency of the reactor system. Then temperature conditions of the reactor system were varied from 10°C to 50°C, the optimum being 30°C. The pH of the media was varied from pH 1 to pH 12, and the optimum pH was found to be 7. The maximum removal efficiency of 77.7% was achieved for synthetic media containing phenol and chromium (VI) in the continuous reactor system at optimized conditions, namely, hydraulic retention time at 4.44 hr, air flow rate at 2.5 lpm, temperature at 30°C, and pH at 7.

Tinospora cordifolia, a novel source of extracellular disaccharidases, useful for human disaccharidase deficiency therapy.

Disaccharide intolerance is the inability to digest certain carbohydrates due to a lack of one or more intestinal disaccharidases (e.g., lactase, maltase, isomaltase and sucrase). Symptoms include diarrhea, abdominal distention and flatulence. Management of the disorder by external enzymes supplementation has not yet been attempted. We report that the medicinal plant Tinospora cordifolia contains substantial amounts of all disaccharidases required for intestinal digestion of carbohydrates. The plant is also a rich source of saccharifying amylase. We recovered (units/100 g fresh stem) amylase: 49,000+500, maltase: 400+50, isomaltase: 130+50, sucrase: 4500+500, acid lactase: 350+30, cellobiase: 35+10 and trehalase: 40+10 by buffer extraction of the blended stem. Crude enzymes in the forms of stem powder, lyophilized aqueous extract and ethanol precipitated protein were found to be stable. Disaccharidases were optimally active at 50 (0) C in the pH range of 4-5. Lactase was an acid lactase similar to the type linked with human lactose intolerance. Enzymes were catalytically stable in the pH range of 2-7 and temperature range of up to 40 (0) C. T. cordifolia enzyme was non-toxic up to a dose of 200 mg protein/kg body weight.

Production, purification, immobilization, and characterization of a thermostable ß-galactosidase from Aspergillus alliaceus.

A fungal strain isolated from rotten banana and identified as Aspergillus alliaceus was found capable of producing thermostable extracellular ß-galactosidase enzyme. Optimum cultural conditions for ß-galactosidase production by A. alliaceus were as follows: pH 4.5; temperature, 30 °C; inoculum age, 25 h; and fermentation time, 144 h. Optimum temperature, time, and pH for enzyme substrate reaction were found to be 45 °C, 20 min, and 7.2, respectively, for crude and partially purified enzyme. For immobilized enzyme-substrate reaction, these three variable, temperature, time, and pH were optimized at 50 °C, 40 min, and 7.2, respectively. Glucose was found to inhibit the enzyme activity. The K(m) values of partially purified and immobilized enzymes were 170 and 210 mM, respectively. Immobilized enzyme retained 43 % of the ß-galactosidase activity of partially purified enzyme. There was no significant loss of activity on storage of immobilized beads at 4 °C for 28 days. Immobilized enzyme retained 90 % of the initial activity after being used four times.

Green pigment from Bacillus cereus M(1)(16) (MTCC 5521): production parameters and antibacterial activity.

A bacterial strain, Bacillus cereus M(1)(16) (MTCC 5521), isolated and identified in our laboratory produces a green pigment when grown in nutrient broth at stationary condition. Optimum fermentation parameters for maximum pigment production are pH 7.0, temperature 30°C, time of incubation 72 h and inoculum volume 1% from 20 h grown cell suspension. Magnesium ion enhances pigment production whereas calcium and zinc ions inhibit the process. The pigment is better extracted from the fermented broth with chloroform in comparison with diethyl ether, ethyl acetate, and butanol. The extracted crude pigment consists of three fractions as revealed from thin layer chromatogram on silica gel GF254 using ethyl acetate and hexane (1:1) solvent system. The major fraction C(3) shows antibacterial activity against different gram positive bacteria. The proposed structure of C(3) is 9-methyl-1,4,5,8-tetra-azaphenanthrene obtained by elemental analysis, GC-MS, and NMR spectra studies.

Adsorption profile of lead on Aspergillus versicolor: a mechanistic probing.

The adsorption of lead on Aspergillus versicolor biomass (AVB) has been investigated in aqueous solution with special reference to binding mechanism in order to explore the possibilities of the biomass to address environmental pollution. AVB, being the most potent of all the fungal biomasses tested, has been successfully employed for reducing the lead content of the effluents of battery industries to permissible limit (1.0 mg L(-1)) before discharging into waterbodies. The results establish that 1.0 g of the biomass adsorbs 45.0 mg of lead and the adsorption process is found to depend on the pH of the solution with an optimum at pH 5.0. The rate of adsorption of lead by AVB is very fast initially attaining equilibrium within 3h following pseudo second order rate model. The adsorption process can better be described by Redlich-Peterson isotherm model compared to other ones tested. Scanning electron micrograph demonstrates conspicuous changes in the surface morphology of the biomass as a result of lead adsorption. Zeta potential values, chemical modification of the functional groups and Fourier transform infrared spectroscopy reveal that binding of lead on AVB occurs through complexation as well as electrostatic interaction.

Beta-D-galactosidase from Enterobacter cloacae: production and some physicochemical properties.

A bacterial strain isolated from soil and identified as Enterobacter cloacae had been found to be capable of producing both intra and extracellular beta-D: -galactosidase.The intracellular enzyme was thermostable and its optimum temperature, pH and time for enzyme-substrate reaction were found to be 50 degrees C, 9.0 and 5 min respectively, using ONPG as substrate. The maximum beta-galactosidase production in shake flask was achieved at 30 degrees C, pH 7.0, incubation time 72 h using 50 ml medium in 250 ml Erlenmeyer flask. Only Mg(2+) stimulated the activity of enzyme. Cetyl trimethyl ammonium bromide showed stimulatory effect on catalytic activity of the enzyme whereas EDTA inhibited enzyme activity. The enzyme retained its activity upto 55 degrees C after incubating at that temperature for 1 h.The maximum activity of crude intracellular enzyme was 14.35 IU/mg of protein. The K (m) and V (max) values of beta-galactosidase using ONPG as substrate at 50 degrees C were 2.805 mM and 37.45 x 10(-3) mM/min/mg, respectively.

Determination of kinetic parameters in the biosorption of Cr (VI) on immobilized Bacillus cereus M(1)(16) in a continuous packed bed column reactor.

Due to technological advancement, environment suffers from untreated toxic heavy metal bearing effluent coming from different industries. Chromium (VI) is one of those heavy metals having adverse impact on ecological balance, human, and plant health because of its carcinogenic properties. Biosorption is presented as an alternative to traditional technologies which are costly and inefficient for treatment of industrial wastes containing low amount of heavy metals. In this study, bioremediation of Cr (VI) ions by immobilized Bacillus cereus M(1) (16) was investigated in a laboratory scale packed bed up-flow column reactor. The effect of important parameters, such as the inlet flow rate, influent concentration, and effective bed height, has been studied. External mass transfer, surface adsorption, and intrabead mass transfer were also studied to conclude the rate limiting step for removal of Cr (VI) and to determine the process parameters which are important for biosorption optimization. The external mass transfer coefficient was calculated at different flow rates (6.51 x 10(-2) to 7.58 x 10(-2) cm/min). Using the model, the surface adsorption rate constant (k(ad)) and the intrabead mass transfer coefficient (k (i)) were predicted as 0.0267 x 10(-3) and 0.7465 x 10(-3) l/g/min, respectively. Both are much lower than the external mass transfer coefficient (k(e)). The surface adsorption phenomenon is acting as the rate-limiting step due to its high resistance for removal of Cr (VI).

Production and characterization of an alkaline thermostable crude lipase from an isolated strain of Bacillus cereus C(7).

A bacterial strain isolated from spoiled coconut and identified as Bacillus cereus was found capable of producing alkaline thermostable extracellular lipase. Optimum temperature, time, and pH for enzyme substrate reaction were found to be 60 degrees C, 10 min, and 8.0 respectively. Common surfactants except Triton X 100 and cetyltrimethylammonium bromide have no or very little inhibitory effects on enzyme activity. The enzyme was found to be stable in presence of oxidizing agents and protease enzyme. The maximum lipase production was achieved at 30-33 degrees C, pH 8.0 on 24 h of fermentation using 50 ml medium in a 250-ml Erlenmeyer flask. The superior carbon and nitrogen sources for lipase production were starch (2%) and ammonium sulfate (nitrogen level 21.2 mg/100 ml), peptone (nitrogen level 297 mg/100 ml), and urea (nitrogen level 46.62 mg/100 ml) in combination, respectively. The maximum enzyme activity obtained was 33 +/- 0.567 IU/ml.

Production of a new antibacterial antibiotic from a mutated strain of Streptomyces kanamyceticus M27 in submerged fermentation.

A new antibacterial antibiotic was produced (136.5 microg/ml) using a 5 L EYELA Fermenter using 2 L fermentation medium at temperature: 27 degrees C, pH: 7.2, agitator speed: 200 rpm, aeration rate 1 vvm having KLa 251.74 hr(-1) at 96 hrs. The optimised conditions for antibiotic using washed cells of the selected strain are pH: 7.2, temperature: 27 degrees C, age of the biomass: 72 hr, amount of washed cell: 4 g in 50 ml normal saline, incubation time 72 hr. The antibacterial activity of the fermented broth was also examined against some bacterial species and it was found that it is active against gram positive as well as gram negative bacteria.

Production of lipase in a fermentor using a mutant strain of Corynebacterium species: its partial purification and immobilization.

Extracellular Corynebacterium lipase was produced using a 2.5 L Chemap fermentor using 1300 ml fermentation medium at temperature 33 degrees C, agitator speed 50 rpm, aeration rate 1 VVM having KLa 16.21 hr(-1). Crude lipase was purified by salting out method followed by dialysis and immobilized using calcium alginate gel matrix followed by glutaraldehyde cross linking Purification process increased specific activity of enzyme from 2.76 to 114.7 IU/mg. Activity of immobilized enzyme was 107.31 IU/mg. Optimum temperature for purified and immobilized enzyme activity were 65 degrees and 50 degrees C respectively. Optimum pH was 8.0 in both the cases, Km and Vmax value for purified lipase were 111.1 micromol/min and 14.7% respectively. Ca2+ (5 mM) was found to be stimulator for enzyme activity. Immobilized lipase retained 68.18% of the original activity when stored for 40 days.