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The carbohydrases of Bacillus stearothermophilus NCIB 11412 and NCIB 10814

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Summary

Two strains (NCIB 11412 and NCIB 10814) of the thermophilic organism Bacillus stearothermophilus were found to produce complex carbohydrase systems. The enzyme activities in each system include α-amylase as the major component, maltase, pullulanase, a minor amylase and cyclodextrinase. The latter three activities are produced in low yield in both strains. A crude enzyme preparation from each strain possessed maltogenic properties on hydrolysis of soluble starch. Following rigorous purification procedures, the purified major α-amylase from either strain did not produce maltose as a major end-product of starch hydrolysis. However, a partially purified mixture of pullulanase, minor amylase and cyclodextrinase activities from NCIB 11412 and NCIB 10814 produced 56.4% and 62.0% maltose, respectively, from soluble starch.

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References

  • Bernfeld P (1955) Amylases α- and β-. Methods Enzymol 1:149–158

    Article  Google Scholar 

  • Brosnan MP, Kelly CT, Fogarty WM (1990) Maltogenic amylases of Bacillus stearothermophilus. Biochem Soc Trans 18:311–312

    Google Scholar 

  • David M-H, Günther H, Röper H (1987) Catalytic properties of Bacillus megaterium amylase. Stärke 39:436–440

    Google Scholar 

  • De Pinto JA, Campbell LL (1968) Purification and properties of the cyclodextrinase of Bacillus macerans. Biochemistry 7:121–125

    Google Scholar 

  • Fogarty WM (1983) Microbial amylases. In: Fogarty WM (ed) Microbial enzymes and biotechnology. Applied Science Publishers, London, pp 1–92

    Google Scholar 

  • Fogarty WM, Kelly CT (1980) Amylases, amyloglocosidases and related glucanases. In: Rose AH (ed) Economic microbiology, vol 5. Microbial enzymes and bioconversions. Academic Press, London, pp 115–170

    Google Scholar 

  • Fogarty WM, Kelly CT (1990) Recent advances in microbial amylases. In: Fogarty WM, Kelly CT (eds) Microbial enzymes and biotechnology, 2nd edn. Elsevier Science Publishers, London, pp 71–132

    Google Scholar 

  • Huggett ASC, Nixon DA (1957) Glucose oxidasemethod for measurement of glucose. Biochem J 6:12–19

    Google Scholar 

  • Imanaka T, Kuriki T (1989) Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan. J Bacteriol 171:369–374

    Google Scholar 

  • Kitahata S, Taniguchi M, Bettran SD, Sugimoto T, Okada S (1983) Purification and some properties of cyclodextrinase from Bacillus coagulans. Agric Biol Chem 47:1441–1447

    Google Scholar 

  • Mielenz JR, Mickel S (1985) Process for cloning the gene coding for a thermostable alpha-amylase into Escherichia coli and Bacillus subtilis. US patent no. 4493 893

  • Oguma T, Kikuchi M, Mizusawa K (1990) Purification and some properties of cyclodextrin hydrolysing enzyme from Bacillus sphaericus. Biochin Biophys Acta 1036:1–5

    Google Scholar 

  • Ohnishi M (1971) Studies on the interaction of substrate analogues with bacterial liquefying α-amylases by means of spectrophotometry and steady state kinetics. J Biochem 69:181–189

    Google Scholar 

  • Outtrup H, Norman BE (1984) Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques. Stärke 36:405–411

    Google Scholar 

  • Plant AR, Clemens RM, Morgan HW, Daniel RM (1987) Activesite and substrate-specificity of Thermoanaerobium Tok6-B1 pullulanase. Biochem J 246:537–541

    Google Scholar 

  • Pollock MR (1961) The measurement of the liberation of penicillinase from B. subtilis. J Gen Microbiol 26:239–253

    Google Scholar 

  • Saha BC, Shen G-J, Srivastava KC, Le Cureux LW, Zeikus JG (1989) New thermostable α-amylase like pullulanase from thermophilic Bacillus sp. 3183. Enzyme Microb Technol 11:760–764

    Google Scholar 

  • Sakano Y, Masuda N, Kobayashi T (1971) Hydrolysis of pullulan by a novel enzyme from Aspergillus niger. Agric Biol Chem 35:971–973

    Google Scholar 

  • Sata H, Umeda M, Kim C-H, Taniguchi H, Maruyama Y (1989) Amylase-pullulanase enzyme produced by B. circulans F-2. Biochim Biophys Acta 991:388–394

    Google Scholar 

  • Sen S, Oriel P (1989) High level extracellular secretion of thermostable α-amylase of Bacillus stearothermophilus in Escherichia coli. Biotechnol Lett 11:383–388

    Google Scholar 

  • Smith PK, Krohn GT, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150:76–85

    CAS  PubMed  Google Scholar 

  • Suzuki Y, Imai T (1985) Bacillus stearothermophilus KP1064 pullulan hydrolase. Appl Microbiol Biotechnol 21:20–26

    Google Scholar 

  • Suzuki Y, Shinji M, Eto N (1984) Assignment of a p-nitrophenyl-α-D-glucopyranosidase of Bacillus stearothermophilus ATCC 12016 to a novel exo-α-1,4-glucosidase active for oligomaltosaccharides and α-glucans. Biochim Biophys Acta 787:281–289

    Google Scholar 

  • Suzuki Y, Nagayama T, Nakano H, Oishi K (1987) Purification and characterization of a maltotriogenic α-amylase I and a maltogenic α-amylase II capable of cleaving α-1,6-bonds in amylopectin. Stärke 39:211–214; 39:246–252

    Google Scholar 

  • Takasaki Y (1987) Pullulanase-amylase complex enzyme from Bacillus subtilis. Agric Biol Chem 51:9–16

    Google Scholar 

Download references

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Fogarty, W.M., Brosnan, M.P., Doyle, E.M. et al. The carbohydrases of Bacillus stearothermophilus NCIB 11412 and NCIB 10814. Appl Microbiol Biotechnol 37, 191–196 (1992). https://doi.org/10.1007/BF00178169

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  • DOI: https://doi.org/10.1007/BF00178169

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