Bacillus amyloliquefaciens

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Bacillus amyloliquefaciens
Scientific classification
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B. amyloliquefaciens
Binomial name
Bacillus amyloliquefaciens
Priest et al., 1987

Bacillus amyloliquefaciens is a species of bacterium in the genus Bacillus that is the source of the BamH1 restriction enzyme. It also synthesizes a natural antibiotic protein barnase, a widely studied ribonuclease that forms a famously tight complex with its intracellular inhibitor barstar, and plantazolicin, an antibiotic with selective activity against Bacillus anthracis.[1]

Discovery and name

B. amyloliquefaciens was discovered in soil 1943 by a Japanese scientist named Fukumoto,[2] who gave the bacterium its name because it produced (faciens) a liquifying (lique) amylase (amylo).

Uses

Alpha amylase from B. amyloliquefaciens is often used in starch hydrolysis. It is also a source of subtilisin, which catalyzes the breakdown of proteins in a similar way to trypsin.

Status as a species

Between the 1940s and the 1980s, bacteriologists debated as to whether or not B. amyloliquefaciens was a separate species or a subspecies of Bacillus subtilis. The matter was settled in 1987: it was established to be a separate species.[3]

In the American Type Culture Collection, the number for B. amyloliquefaciens is 23350.

References

  1. ^ Molohon KJ, Melby JO, Lee J, Evans BS, Dunbar KL, Bumpus SB, Kelleher NL, Mitchell DA (2011). “Structure Determination and Interception of Biosynthetic Intermediates for the Plantazolicin Class of Highly Discriminating Antibiotics”. ACS Chem. Biol. 6 (12): 1307-1313. doi: 10.1021/cb200339d. PMID 21950656.
  2. ^ J. Fukumoto (1943). "Studies on the production of bacterial amylase. I. Isolation of bacteria secreting potent amylases and their distribution". Journal of the Agricultural Chemical Society of Japan (in Japanese). 19: 487–503.
  3. ^ *F. G. Priest; M. Goodfellow; L. A. Shute; R. C. W. Berkeley (1987). "Bacillus amyloliquefaciens sp. nov., nom. rev". International Journal of Systematic Bacteriology. 37 (1): 69–71. doi:10.1099/00207713-37-1-69.