Bacillus acidocaldarius sp.nov., an Acidophilic Thermophilic Spore-forming Bacterium

Darland, Gary; Brock, Thomas D.

doi:10.1099/00221287-67-1-9

Cited by 262 publications

(125 citation statements)

References 10 publications

(4 reference statements)

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“…Cells of A. acidoterrestris were pre-cultured at 43 C for 4 h in 10 mL Bacillus acidoterrestris broth (BAT, D€ ohler, Germany) to achieve a cell density of approximately 10 6 e10 7 CFU/mL. Then, 100 mL culture was spread onto Bacillus acidoterrestris agar (BATA, Merck), Bacillus acidocaldarius agar (BAA), (Darland & Brock, 1971), potato dextrose agar (PDA, BD Difco), malt extract agar (MEA, Oxoid). All inoculated plates were incubated at 43 C. Sporulation was determined by direct observation of free, fully refractile spores under the phase-contrast microscope (Olympus CX31, Japan).…”

Section: Microorganism and Spore Productionmentioning

confidence: 99%

Antimicrobial activity of grape seed extract on Alicyclobacillus acidoterrestris DSM 3922 vegetative cells and spores in apple juice

Molva

Baysal

2015

LWT - Food Science and Technology

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Chemical compounds studied in this article: Grape seed extract (proanthocyanidins) (PubChem CID: 108065) gallic acid (PubChem CID: 370) disodium carbonate (PubChem CID: 10340) sodium acetate trihydrate (PubChem CID: 23665405) 2,4,6-tripyridyl-s-triazine (PubChem CID: 77258) iron chloride (PubChem CID: 24380) a b s t r a c tThe present study evaluated the antimicrobial activity of grape seed extract (GSE) against Alicyclobacillus acidoterrestris vegetative cells and spores in apple juice (pH 3.82, Brix 11.3) during storage at 37 C. After 336 h, reductions in the cell numbers were 3.14, 3.55, 3.8, 4.1, and 4.63 log CFU/mL in the apple juice with 0.23, 0.45, 0.9, 1.8, and 3.6% of GSE, respectively. The Weibull was found to be the best fitted model for cell inactivation kinetics (R 2 > 0.988). Moreover, the spores produced on different sporulation media (potato dextrose agar, malt extract agar, Bacillus acidoterrestris agar, and Bacillus acidocaldarius agar) were treated with GSE (0e1.9%, v/v). While control spores in apple juice without GSE increased by 2.2e2.6 log CFU/mL within the first 48 h, 0.9% and 1.8% of GSE inhibited the growth from all spore suspensions. Finally, scanning electron microscopy (SEM) indicated that the main target of the GSE may be the membrane of A. acidoterrestris cells leading to leakage of cellular constituents and may prevent the development of spores into vegetative cells. This study highlights the potential use of the by-products of the fruit juice/ beverage industry as natural antimicrobials to inhibit the growth of A. acidoterrestris.

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Section: Microorganism and Spore Productionmentioning

confidence: 99%

Antimicrobial activity of grape seed extract on Alicyclobacillus acidoterrestris DSM 3922 vegetative cells and spores in apple juice

Molva

Baysal

2015

LWT - Food Science and Technology

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“…Batch cultures of cells were grown at 57 "C under vigorous agitation in a 500-ml Erlenmeyer flask containing 200 ml medium of the following composition: 9.8 mM (NH4)*S04, 0.47 mM CaCl,, 2.7 mM KH,PO, and 1.0 mM MgSOd, pH 3.5 (adjusted with HCl). The sterile medium was supplemented with 10 pM FeSO, and the following trace element salts: 9.1 pM MnCl,, 11.7 pM NaB,O,, 0.57 pM ZnSO,, 0.2 pM CuCl,, 0.12 pM VOSO,, 30.0 nM CoSO, and 0.16 pM NaMoO, [9,301. The carbon source was 10 mM glucose, 10 mM maltose, 20 mM glycerol or 1% (mass/vol.)…”

Section: Organism and Culture Conditionsmentioning

confidence: 99%

Purification, Properties and Structural Aspects of a Thermoacidophilic α‐Amylase from Alicyclobacillus Acidocaldarius Atcc 27009

Schwermann

Pfau

Liliensiek

et al. 1994

European Journal of Biochemistry

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The a-amylase from the thermoacidophilic eubacterium Alicyclobacillus (Bacillus) acidocaldarius strain ATCC 27009 was studied as an example of an acidophilic protein. The enzyme was purified from the culture fluid. On an SDS/polyacrylamide gel, the protein exhibited an apparent molecular mass of 160 kDa, which is approximately 15% higher than that predicted from the nucleotide sequence. The difference is due to the enzyme being a glycoprotein. Deglycosylation or synthesis of the enzyme in Escherichia coli gave a product with the mass expected for the mature protein.The amylase hydrolyzed starch at random and from the inside, and its main hydrolysis products were maltotriose and maltose. It also formed glucose from starch (by hydrolysing the intermediate product maltotetraose to glucose and maltotriose) and exhibited some pullulanase activity. The pH and temperature optima were pH 3 and 75 "C, respectively, characterizing the enzyme as being thermoacidophilic. Alignment of the sequence of the enzyme with that of its closests neutrophilic relatives and with that of a-1,4 or a-1,6 glycosidic-bond hydrolyzing enzymes of known threedimensional structure showed that the acidophilic a-amylase contains approximately 30% less charged residues than do its closests relatives, that these residues are replaced by neutral polar residues, and that hot spots for these exchanges are likely to be located at the surface of the protein.Literature data show that similar effects are observed in three other acidophilic proteins. It is proposed that these proteins have adapted to the acidic environment by reducing the density of both positive and negative charges at their surface, that this effect circumvents electrostatic repulsion of charged groups at low pH, and thereby contributes to the acidostability of these proteins.Enzymes optimally active under extreme conditions are both of biotechnological importance and of scientific interest (for reviews see [I-31). Much work has been devoted to the mechanism of thermostability. However, its outcome is complex. Theoretical considerations suggest that the exchange of a single amino acid residue in an enzyme can increase its temperature optimum by more than 10°C [3]. Studies on forced molecular evolution have provided support for this notion. In such thermo-drill experiments, a gene encoding a mesophilic enzyme is introduced into a thermophilic organism, and by gradually increasing the growth tem-Correspondence to E. P. Bakker, Abteilung Mikrobiologie,

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“…Autotrophic growth of other bacilli Other bacilli possessing characteristics in common with strains MA48 and MA51 were tested for autotrophic growth under H2/0,/C02 at their respective temperature and pH optima. These included thermophilic strains of Bacillus sphaericus (Hollaus & Klaushofer, 1970) as well as mesophilic strains of the same species previously attributed to B. pycnoticus (R. E. Gordon, personal communication), B. thermoruber (Guicciardi et al, 1968 ;Aragozzini et al, 1976) and B. acidocaldarius (Darland & Brock, 1971). None of these strains were able to develop autotrophically.…”

Section: New T H Ermop H Ilic H Y Dr Og En-oxidizing Bacillus 337mentioning

confidence: 99%

Bacillus schlegelii, a New Species of Thermophilic, Facultatively Chemolithoautotrophic Bacterium Oxidizing Molecular Hydrogen

Schenk

Aragno

1979

Journal of General Microbiology

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Bacillus acidocaldarius sp.nov., an Acidophilic Thermophilic Spore-forming Bacterium

Cited by 262 publications

References 10 publications

Antimicrobial activity of grape seed extract on Alicyclobacillus acidoterrestris DSM 3922 vegetative cells and spores in apple juice

Antimicrobial activity of grape seed extract on Alicyclobacillus acidoterrestris DSM 3922 vegetative cells and spores in apple juice

Purification, Properties and Structural Aspects of a Thermoacidophilic α‐Amylase from Alicyclobacillus Acidocaldarius Atcc 27009

Bacillus schlegelii, a New Species of Thermophilic, Facultatively Chemolithoautotrophic Bacterium Oxidizing Molecular Hydrogen

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