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  • 1
    Electronic Resource
    Electronic Resource
    Cloning and expression of a thermostable exo-α-1,4-glucosidase gene from Bacillus stearothermophilus ATCC12016 in Escherichia coli (1992)
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 243-247 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The gene coding for a thermostable exo-α-1,4-glucosidase (α-glucoside glucohydrolase: EC 3.2.1.20) of Bacillus stearothermophilus ATCC 12016 was cloned within a 2.8-kb AvaI fragment of DNA using the plasmid pUC19 as a vector and Escherichia coli JM109 as a host. E. coli with the hybrid plasmid accumulated exo-α-1,4-glucosidase mainly in the cytoplasm. The level of enzyme production was about sevenfold higher than that observed for B. stearothermophilus. The cloned enzyme coincided absolutely with the B. stearothermophilus enzyme in its relative molecular mass (62 000), isoelectric point (5.0), amino-terminal sequence of 15 residues (Met-Lys-Lys-Thr-Trp-Trp-Lys-Glu-Gly-Val-Ala-Tyr-Gln-Ile-Tyr-), the temperature dependency of its activity and stability, and its antigenic determinants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00174476
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  • 2
    Electronic Resource
    Electronic Resource
    Alkaline serine protease produced from citric acid by Bacillus alcalophilus subsp. halodurans KP 1239 (1990)
    Springer
    Applied microbiology and biotechnology 34 (1990), S. 57-62 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Maximum production of alkaline serine protease by Bacillus alcalophilus subsp. halodurans KP 1239 was achieved after 24 h cultivation, at an initial pH of 7.6, on a medium containing 1.0% sodium citrate, 0.3% yeast extract, and 0.3% KH2PO4. The enzyme was purified to crystalline form from culture broth. The enzyme was most active at 60° C and at pH 11.5. The molecular weight, isoelectric point and sedimentation coefficient in water at 20° C were estimated as 29 000, 8.8 and 3.3S, respectively. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg-Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-. The enzyme shared its antigenic determinants with B. alcalophilus ATCC 21522 serine protease, but not with the subtilisins Carlsberg and BPN′.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170924
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  • 3
    Electronic Resource
    Electronic Resource
    A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 546-551 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A p-nitrophenyl-α-d-glucopyranoside-hydrolysing oligo-1,6-glucosidase (dextrin 6-α-d-glucanohydrolase, EC 3.2.1.10) of Bacillus sp. KP 1071 capable of growing at 30°–66°C was purified to homogeneity. The molecular weight was estimated to be 62,000. The amino-terminal amino acid was methionine. The enzyme shared its antigenic groups in part with its homologous counterpart from Bacillus thermoglucosidasius KP 1006 (obligate thermophile), but did not at all with any one of oligo-1,6-glucosidases from Bacillus cereus ATCC 7064 (mesophile), Bacillus coagulans ATCC 7050 (facultative thermophile) and Bacillus flavocaldarius KP 1288 (extreme thermophile). A comparison of amino acid composition showed that the proline content increased greatly in a linearity with the rise in thermostability in the order, mesophile → facultative thermophile → KP 1071 → obligate thermophile → extreme thermophile enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253030
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  • 4
    Electronic Resource
    Electronic Resource
    Bacillus stearothermophilus KP 1236 neutral protease with strong thermostability comparable to thermolysin (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 186-191 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An extracellular neutral protease, of Bacillus stearothermophilus KP 1236 (a soil isolate) able to grow at 39°–71°C was purified to homogeneity. The molecular weight, sedimentation coefficient in water at 20°C, and isoelectric point were estimated as 33,000, 3.46 S and 7.5, respectively. The enzyme was most active at 80°C and pH 7.0. The activity was stable for 10 min up to 80°C at pH 7.5 and for 18 h at 60°C over pH 6.0–8.8. The enzyme and thermolysin (microbial metalloproteinase, EC 3.4.24.4) shared their antigenic determinants in part.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251943
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  • 5
    Electronic Resource
    Electronic Resource
    A relationship between efficiency of isomaltosaccharide hydrolysis and thermostability of six Bacillus oligo-1,6-glucosidases (1989)
    Springer
    Applied microbiology and biotechnology 31 (1989), S. 32-37 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A p-nitrophenyl-α-d-glucopyranosidase from Bacillus thermoamyloliquefaciens KP 1171 capable of growing at 30°–66°C was assigned to an oligo-1,6-glucosidase (dextrin 6-α-d-glucanohydrolase, EC 3.2.1.10). The enzyme was compared with its homologous counterparts from B. cereus NY-14, B. cereus ATCC 7064 (each mesophile), B. coagulans ATCC 7050 (facultative thermophile), B. thermoglucosidasius KP 1006 (DSM 2542, obligate thermophile) and B. flavocaldarius KP 1228 (extreme thermophile) in thermostability and kinetic parameters at suboptimal temperatures for isomaltosaccharides (2–6 glucose units). This analysis showed that the efficiency of each isomaltosaccharide hydrolysis changes in a convex manner with increasing thermostability on the transition, NY-14 → ATCC 7064 → ATCC 7050 → KP 1071 → KP 1006 → KP 1228 enzymes, with a maximum at KP 1071 or ATCC 7050 enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252522
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  • 6
    Electronic Resource
    Electronic Resource
    A hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability (1991)
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 707-714 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A cell-associated pullalanase (α-dextrin 6-glucanohydrolase, EC 3.2.1.41) of an extreme thermophile, Bacillus flavocaldarius KP 1228, was purified to homogeneity. The molecular weight and isoelectric point were estimated to be about 55 000 and 7.0, respectively. The N-terminal sequence was Ala-Try-Tyr-Glu-Gly-Ala-Phe-Phe-Tyr-Gln-Ile-Phe-Pro-Asp-Tyr-Phe-Phe-Tyr-Ala-Gly-. The enzyme was most active at pH 6.3. The activities for 5% pullulan and 5% soluble starch were maximal at 75–80° C and at 80–85° C, respectively. The enzyme was stable up to 90° C for 10 min at pH 6.8. The enzyme had no antigenic determinants shared with pullulanases from the mesophiles Klebsiella pneumoniae and B. acidopullulyticus NCIB 11647. A comparison of amino acid composition demonstrated that the proline content increased greatly in a linear fashion with the rise in thermostability in the order K. pneumoniae → B. acidopullulyticus → B. flavocaldarius enzymes, as found with Bacillus oligo-1,6-glucosidases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169338
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  • 7
    Electronic Resource
    Electronic Resource
    Bacillus stearothermophilus KP 1064 pullulan hydrolase (1985)
    Springer
    Applied microbiology and biotechnology 21 (1985), S. 20-26 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A pullulan hydrolase of Bacillus stearothermophilus KP 1064 was purified homogeneously. The molecular weight, Stokes radius, sedimentation coefficient (s20, w), extinction coefficient at 280 nm and pH 6.8, and isoelectric point were estimated as 115,000, 4.16 nm, 5.5 S, 1.92 cm2·mg-1 and 4.4, respectively. The enzyme consisted of two identical subunits each comprising a methionine residue at the NH2-terminus. The enzyme hydrolysed pullulan, amylopectin, soluble starch, amylose, α-and β-limit dextrins, α- and β-cyclodextrins, phenylα-d-maltoside, maltotriose, and maltopentaose. The main products from amylose and pullulan were maltose and panose, respectively. The substrate specificity, along with the pattern of products, suggested the assignment of the enzyme to a unique type of maltogenic α-amylase (1,4α-d-glucan glucanohydrolase, EC. 3.2.1.1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252356
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  • 8
    Electronic Resource
    Electronic Resource
    Production of extracellular thermostable pullulanase by an amylolytic obligately thermophilic soil bacterium, Bacillus stearothermophilus KP 1064 (1983)
    Springer
    Applied microbiology and biotechnology 17 (1983), S. 24-29 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An amylolytic obligate thermophile producing high amounts of extracellular pullulanase was isolated from soil. The isolate (KP 1064) that grew from 45°C to 69°C was identified as a strain of Bacillus stearothermophilus. Maximal enzyme activity was achieved after 18 h of shaking cultivation at 60°C and at an initial pH of 7.1–7.5, on a medium composed of 1.2% (w/v) soluble starch, 1.4%–1.6% peptone, 0.3% yeast extract, 0.3% K2HPO4, and 0.1% KH2PO4. Pullulanase synthesis was significantly enhanced by dextrin, amylopectin, soluble starch as well as maltose, but not at all by pullulan. A large enzyme accumulation in the culture broth took place in the early stationary phase of growth, but the exoenzyme activity rapidly disappeared in the late stage of this period with a rate of 0.074 unit decreased/ml of culture/10h.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00510567
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  • 9
    Electronic Resource
    Electronic Resource
    The lack of identity between Bacillus stearothermophilus and Bacillus thermoglucosidasius in serological patterns of exo-oligo-1,6-glucosidase and exo-α-1,4-glucosidase (1984)
    Springer
    Applied microbiology and biotechnology 20 (1984), S. 218-220 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Among 16 Bacillus stearothermophilus strains, 11 strains (ATCC 7953, ATCC 10149, ATCC 12976, ATCC 12978, ATCC 12980, ATCC 15951, ATCC 21365, IAM 11001, IAM 11004, IAM 11062 and IFO 12550) produced a protein reactable on double immuno-diffusion with the antiserum against Bacillus thermoglucosidasius KP 1006 (DSM 2542) exo-oligo-1,6-glucosidase (dextrin 6-glucanohydrolase, EC.3.2.1.10). However, these antigens in part shared their antigenic determinants. In addition to an exo-oligo-1,6-glucosidase, 6 B. thermoglucosidasius strains [KP 1006, KP 1012, KP 1013, KP 1014, KP 1019 and KP 1022 (DSM 2543)] formed a protein cross-reacted with the antiserum against B. stearothermophilus ATCC 12016 exo-α-1,4-glucosidase (α-d-glucoside glucohydrolase, EC.3.2.1.20). These two antigens showed, however, a partial coincidence in their antigenic determinant groups. Of 16 B. stearothermophilus strains, 3 strains (ATCC 8005, ATCC 12016 and ATCC 15952) produced a protein immunologically compatible with the α-1,4-glucosidase, while 4 strains (ATCC 12979, ATCC 12980, ATCC 15951 and IAM 11001) made the other protein which showed certain differences partly from this enzyme in its antigenic groups. No protein precipitated with the anti-α-1,4-glucosidase occurred in the remaining 9 B. stearothermophilus strains (ATCC 7953, ATCC 10149, ATCC 12976, ATCC 12977, ATCC 12978, ATCC 21365, IAM 11004, IAM 11062 and IFO 12550). These data indicate no serological identity between two thermophilic Bacillus species in their glucosidase patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253734
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  • 10
    Electronic Resource
    Electronic Resource
    A simplified method of the purification of Bacillus cereus ATCC 7064 exo-oligo-1,6-glucosidase by the use of immunosorbent (1983)
    Springer
    Applied microbiology and biotechnology 18 (1983), S. 254-256 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A p-nitrophenyl-α-D-glucopyranoside-hydrolyzing exo-oligo-1,6-glucosidase (dextrin 6-α-glucanohydrolase, EC.3.2.1.10) of Bacillus cereus ATCC 7064 was 1,120-fold purified to an electrophoretically- and immunologically-homogeneous form by a simple 4-step method containing as the most efficient step the enzyme elution from immunosorbent with a pH 11 medium including 50% (w/v) glycerol. The final enzyme yield was 47%. The specific activity was 218 μmol p-nitrophenyl-α-D-glucopyranoside hydrolyzed/min/mg protein at 35°C and pH 6.8. The amino-terminal amino acid of the enzyme was determined to be methionine. No antigenic common determinant occurred between this enzyme and each of its homologous counterparts from obligate thermophile Bacillus thermoglucosidius KP 1006 and from facultative thermophile Bacillus coagulans ATCC 7050.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00501519
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