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Neil E. Welker - One of the best experts on this subject based on the ideXlab platform.
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New shuttle vector for cloning in Bacillus Stearothermophilus
Research in Microbiology, 1994Co-Authors: E. Rossi, Patrizia Brigidi, Giovanna Riccardi, Neil E. Welker, Diego MatteuzziAbstract:Abstract Cloning vector plasmid pRP9 was constructed on the basis of the broad host-range plasmid pLM6. pRP9 was a small plasmid (2.9 kb), possessed a convenient polyrestriction site sequence and efficiently transformed Bacillus subtilis, Bacillus Stearothermophilus and Escherichia coli . Furthermore, pRP9 presented a very high segregational stability in Bacillus hosts. Also, the structural stability in Bacillus strains, grown under selective pressure, of pRP9 carrying a 3-kb fragment, was high. No single-stranded and high-molecular weight pRP9 DNA was found in B. Stearothermophilus . The host/vector systems described possessed all the properties required for efficient gene cloning.
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The Genetic Map of Bacillus Stearothermophilus
Bacillus subtilis and Other Gram-Positive Bacteria, 1993Co-Authors: Neil E. WelkerAbstract:Although some progress has been made in the development of genetic technology for Bacillus Stearothermophilus, strains of the genus Thermus, and Methanobacterium thermoautotrophicum, the lack of efficient and reliable genetic exchange systems, a repertoire of mutants, or plasmids that express useful genetic markers has hampered the exploitation of these organisms for basic and applied research. Recent progress in the development of genetic techniques for B. Stearothermophilus NUB36 makes it possible to elucidate the molecular and genetic mechanisms of thermophily in this organism. The genetic characterization of the B. Stearothermophilus NUB36 genome is the first step in attaining this goal. The map was constructed using the linkages reported by Vallier and Welker. The genetic map of B. Stearothermophilus NUB36 may be similar to the B. subtilis 168 map; however, the identity of the genes in B. Stearothermophilus with the putative analogous genes of B. subtilis must be rigorously established by biochemical and molecular biological techniques.
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Temperature-induced protein synthesis in Bacillus Stearothermophilus NUB36.
Journal of Bacteriology, 1991Co-Authors: Neil E. WelkerAbstract:Cultures of Bacillus Stearothermophilus subjected to a temperature shift-up or shift-down of 15 degrees C within the normal temperature range of growth (45 to 65 degrees C) enter a transient adaptation period before exponential growth at the new temperature. The de novo synthesis of some proteins coincides with the adaptation period.
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Genetic map of the Bacillus Stearothermophilus NUB36 chromosome.
Journal of Bacteriology, 1990Co-Authors: H Vallier, Neil E. WelkerAbstract:A circular genetic map of Bacillus Stearothermophilus NUB36 was constructed by transduction with bacteriophage TP-42C and protoplast fusion. Sixty-four genes were tentatively assigned a cognate Bacillus subtilis gene based on growth response to intermediates or end products of metabolism, cross-feeding, accumulation of intermediates, or their relative order in a linkage group. Although the relative position of many genes on the Bacillus Stearothermophilus and Bacillus subtilis genetic map appears to be similar, some differences were detected. The tentative order of the genes in the Bacillus Stearothermophilus aro region is aspB-aroBAFEC-tyrA-hisH-(trp), whereas it is aspB-aroE-tyrA-hisH-(trp)-aroHBF in Bacillus subtilis. The aroA, aroC, and aroG genes in Bacillus subtilis are located in another region. The tentative order of genes in the trp operon of Bacillus Stearothermophilus is trpFCDABE, whereas it is trpABFCDE in Bacillus subtilis.
T Leighton - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Bacillus Stearothermophilus 30S and 50S ribosomal protein mutations.
Journal of Bacteriology, 1990Co-Authors: J Schnier, H S Gewitz, S E Behrens, A Lee, C Ginther, T LeightonAbstract:Bacillus Stearothermophilus mutations which confer resistance to or dependence on a variety of ribosome-targeted antibiotics have been isolated. Many of these mutations produce ribosomal proteins with altered mobilities in a two-dimensional gel electrophoresis system. This collection of altered thermophilic ribosomal proteins will be useful in examining ribosomal structure and function.
Kwan-hwa Park - One of the best experts on this subject based on the ideXlab platform.
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Transglycosylation of Neohesperidin Dihydrochalcone by Bacillus Stearothermophilus Maltogenic Amylase
Journal of Agricultural and Food Chemistry, 2000Co-Authors: Tae Kyou Cheong, Kwan-hwa ParkAbstract:Neohesperidin dihydrochalcone (NHDC), a sweet compound derived from citrus fruits, was modified to a series of its oligosaccharides by transglycosylation activity of Bacillus Stearothermophilus maltogenic amylase (BSMA). Maltotriose as a donor was reacted with NHDC as an acceptor to glycosylate for the purpose of increasing the solubility of NHDC. Maltosyl-NHDC was a major transglycosylation product among the several transfer products by TLC analysis. The structure of the major transglycosylation product was determined to be maltosyl-α-(1,6)-neohesperidin dihydrochalcone by MALDI-TOF/MS and 1H and 13C NMR. Maltosyl-NHDC was 700 times more soluble in water and 7 times less sweet than NHDC. Keywords: Bacillus Stearothermophilus maltogenic amylase (BSMA); transglycosylation; neohesperidin dihydrochalcone (NHDC); maltosyl-α-(1,6)-neohesperidin dihydrochalcone
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Transglycosylation of naringin by Bacillus Stearothermophilus maltogenic amylase to give glycosylated naringin
Journal of Agricultural and Food Chemistry, 1999Co-Authors: So Jin Lee, Jae-cherl Kim, Myo Jeong Kim, Motomitsu Kitaoka, Cheon-seok Park, Suyong Lee, Tae Wha Moon, John F. Robyt, Kwan-hwa ParkAbstract:Naringin, a bitter compound in citrus fruits, was transglycosylated by Bacillus Stearothermophilus maltogenic amylase reaction with maltotriose to give a series of mono-, di-, and triglycosylnaringins. Glycosylation products of naringin were observed by TLC and HPLC. The major glycosylation product was purified by using a Sephadex LH-20 column. The sturcture was determined by using MALDI-TOF MS, methylation analysis, and 1H and 13C NMR. The major transglycosylation product was maltosylnaringin, in which the maltose unit was attached by an α-1→6 glycosidic linkage to the d-glucose moiety of naringin. This product was 250 times more soluble in water and 10 times less bitter than naringin. Keywords: Naringin; maltogenic amylase from Bacillus Stearothermophilus; maltosylnaringin; transglycosylation
J Schnier - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Bacillus Stearothermophilus 30S and 50S ribosomal protein mutations.
Journal of Bacteriology, 1990Co-Authors: J Schnier, H S Gewitz, S E Behrens, A Lee, C Ginther, T LeightonAbstract:Bacillus Stearothermophilus mutations which confer resistance to or dependence on a variety of ribosome-targeted antibiotics have been isolated. Many of these mutations produce ribosomal proteins with altered mobilities in a two-dimensional gel electrophoresis system. This collection of altered thermophilic ribosomal proteins will be useful in examining ribosomal structure and function.
H Zhang - One of the best experts on this subject based on the ideXlab platform.
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immobilization of recombinant thermostable β galactosidase from Bacillus Stearothermophilus for lactose hydrolysis in milk
Journal of Dairy Science, 2009Co-Authors: Wei Chen, Haiqin Chen, Jiayu Yang, J Zhao, Fengwei Tian, H P Zhang, H ZhangAbstract:Abstract A recombinant thermostable β-galactosidase from Bacillus Stearothermophilus was immobilized onto chitosan using Tris(hydroxymethyl)phosphine (THP) and glutaraldehyde, and a packed bed reactor was utilized to hydrolyze lactose in milk. The thermostability and enzyme activity of THP-immobilized β-galactosidase during storage was superior to that of free and glutaraldehyde-immobilized enzymes. The THP-immobilized β-galactosidase showed greater relative activity in the presence of Ca 2+ than the free enzyme and was stable during the storage at 4°C for 6 wk, whereas the free enzyme lost 31% of the initial activity under the same storage conditions. More than 80% of lactose hydrolysis in milk was achieved after 2h of operation in the reactor. Therefore, THP-immobilized recombinant thermostable β-galactosidase from Bacillus Stearothermophilus has the potential for application in the production of lactose-hydrolyzed milk.
