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J N Baruah

Publications and source records attributed to J N Baruah.

At least 19 recordsLinked to original sources
PubMed1988

Effect of growth temperature and media composition on the fatty acid composition of Bacillus stearothermophilus AN 002.

The influence of growth temperature, media composition and cell age on the chemical composition of Bacillus stearothermophilus strain AN 002 has been determined. The total cellular protein decreased and the free amino acid content increased with growth temperature, in both exponential and stationary growth phase. The protein and free amino acid contents of cells were higher in the stationary phase than in the exponential phase, irrespective of growth temperature and media composition. The RNA content was only reduced in cells grown at 55 degrees C. No significant variations were observed in the DNA and carbohydrate contents with respect to growth temperature and cell age. The total lipid and fatty acid compositions on the other hand varied as a function of growth temperature, cell age and media composition. Differences in the relative concentrations of even, odd and branched chain fatty acids were noticed. No variation was observed in the antiiso and unsaturated fatty acids with respect to growth temperature. The unique variations in the fatty acid composition and total lipids at the growth temperature of 50 degrees C and their variations in the stationary growth phase seem to be characteristic for B. stearothermophilus AN 002.

Amino Acids↗
PubMed1986

Culture Conditions for Production of Thermostable Amylase by Bacillus stearothermophilus.

Bacillus stearothermophilus grew better on complex and semisynthetic medium than on synthetic medium supplemented with amino acids. Amylase production on the complex medium containing beef extract or corn steep liquor was higher than on semisynthetic medium containing peptone (0.4%). The synthetic medium, however, did not provide a good yield of extracellular amylase. Among the carbohydrates which favored the production of amylase are, in order starch > dextrin > glycogen > cellobiose > maltohexaose-maltopeptaose > maltotetraose and maltotriose. The monosaccharides repressed the enzyme production, whereas inositol and d-sorbitol favored amylase production. Organic and inorganic salts increased amylase production in the order of KCI > sodium malate > potassium succinate, while the yield was comparatively lower with other organic salts of Na and K. Amino acids, in particular isoleucine, cysteine, phenylalanine, and aspartic acids, were found to be vital for amylase synthesis. Medium containing CaCl(2) 2H(2)O enhanced amylase production over that on Ca -deficient medium. The detergents Tween-80 and Triton X-100 increased biomass but significantly suppressed amylase synthesis. The amylase powder obtained from the culture filtrate by prechilled acetone treatment was stable over a wide pH range and liquefied thick starch slurries at 80 degrees C. The crude amylase, after (NH(4))(2)SO(4) fractionation, had an activity of 210.6 U mg. The optimum temperature and pH of the enzyme were found to be 82 degrees C and 6.9, respectively. Ca was required for the thermostability of the enzyme preparation.

Journal Article↗
PubMed1984

Factors limiting the microbial conversion of sterols to 17-ketosteroids in the presence of metal chelate inhibitors.

Bioconversion of sterols to 17-ketosteroids by an Arthrobacter species occurred in the presence of hydrophobic metal-chelating agents but the production of 17-ketosteroids (17-KS) was seriously limited by the rapid loss of the viability of cells in the presence of these inhibitors. Besides, the conversion was inhibited by 17-KS at concentrations of 500 ppm or more. The 17-KS formed consisted exclusively of 1,4-androstadiene-3,17-dione (ADD) and 4-androstene-3,17-dione (AD) and these were found in the extracellular medium predominantly in bound form or as molecular aggregates which may limit their accumulation. It was concluded that enhanced production of 17-KS could be achieved by protecting the viability of cells and by removing the steroid metabolites from the site of inhibition.

17-Ketosteroids↗
PubMed1984

Partial purification and properties of thermostable intracellular amylases from a thermophilic Bacillus sp. AK-2.

Intracellular thermostable amylases from a thermophilic Baccilus sp. AK-2 have been isolated and purified. The crude enzyme, having pH optimum at 6.5. and temperature optimum at 68 degrees C was purified by DEAE-cellulose column chromatography. Three separable enzyme fractions having starch hydrolyzing property were eluted by lowering the pH from 8.5 to 7.0. Electrophoretic mobility of these fractions showed a single band. Calcium ion up to a concentration of 20 mM had an activating effect on the three fractions. The optimum temperature for the three fractions (FI, FII and FIII) was 65 degrees C and the pH optimum for each was 6.0, 6.5 and 6.0, respectively. The -SH group in the amylase molecule was essential for enzyme activity. Except for Ca2+, Mg2+, Sr2+ and Mn2+ all other metal ions studied inhibited both alpha and beta-amylase activities. EDTA showed dose dependent non-competitive inhibition. Product formation studies proved FI and FIII to be of the alpha-amylase type and FII of the beta-amylase type. The Km for the substrate (starch) in the presence or absence of EDTA was 0.8 X 10(-3) and 1.13 X 10(-3) g/ml for alpha-amylase and beta-amylase, respectively.

Amylases↗
PubMed1981

Effect of carbon and nitrogen sources on neutral proteinase production by Pseudomonas aeruginosa.

A strain of Pseudomonas aeruginosa from soil produced large quantities of extracellular neutral proteinase and could utilize several organic substances as carbon and nitrogen sources for enzyme production. The growth media required the presence of a high amount of phosphate when glucose was the carbon source. The intermediates of citric-acid cycle acids supported the proteinase production more than any other carbon sources. However, complex nitrogenous substances supported enzyme production more efficiently. Higher concentration of casamino acids suppressed the protinase synthesis.

Acids↗