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  • 1
    Electronic Resource
    Electronic Resource
    Production of β-mannosidase and β-mannanase by an alkalophilic Bacillus sp. (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 323-327 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An alkalophilic bacterium producing high amounts of the cell-associated β-mannosidase and extracellular β-mannanase was isolated from soil. The isolate (AM-001) that grew well in alkaline pH media was identified as a strain of Bacillus sp. The optimal cultivation temperature for enzyme production was 31° C for β-mannosidase and 37° C for β-mannanase with the optimum production medium composed of 1% konjac powder, 0.2% yeast extract, 2% Polypepton, 0.1% K2HPO4, 0.02% MgSO4 · 7H2O and 0.5% Na2CO3. Optimum pH and temperature for β-mannosidase were 7.0 and 55° C, and for β-mannanase were 9.0 and 65° C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256662
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  • 2
    Electronic Resource
    Electronic Resource
    The cloned β-mannanase gene from alkalophilic Bacillus sp. AM-001 produces two β-mannanases in Escherichia coli (1989)
    Springer
    Archives of microbiology 152 (1989), S. 10-15 
    Details
    ISSN: 1432-072X
    Keywords: Alkalophilic Bacillus sp. ; β-Mannanase gene ; Escherichia coli ; Cloning ; Expression ; β-Mannanase ; Southern hybridization ; Western blotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding β-mannanase was cloned from alkalophilic Bacillus sp. AM-001 into Escherichia coli JM 101 by inserting HindIII-generated DNA fragments into the HindIII site of pUC19. A 2.0 kb XbaI-PstI fragment of the donor strain DNA was sufficient for β-mannanase synthesis. The amount of β-mannanase expressed in E. coli JM101 harboring pMAH3 (containing a 2.4 kb XbaI-HindIII fragment) was about 24% of the activity produced by the donor strain. E. coli JM101 harboring pMAH3 was found to produce two enzymatically active β-mannanases (A and B). These two β-mannanases were purified to electrophoretically homogenous states. The β-mannanase A had enzymatic properties similar to those of the β-mannanases M-I and M-II produced by alkalophilic Bacillus sp. AM-001, and the β-mannanase B resembled its β-mannanase M-III. In contrast to β-mannanase production in the donor strain, that in E. coli was not inducible. The NH2-terminal amino acid sequences from amino acid 1 (Asn) to 9 (Gln) of the three β-mannanases purified from alkalophilic Bacillus sp. AM-001 coincide with those from amino acid 4 (Asn) to 12 (Gln) of the two β-mannanases purified from E. coli transformant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447004
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    Paper (German National Licenses)
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