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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1961 4
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1975 1
1976 1
1978 1
1980 1
1981 1
1982 1
1983 2
1984 1
1985 5
1986 3
1987 6
1988 5
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1990 10
1991 7
1992 2
1993 6
1994 3
1995 3
1996 4
1997 3
1998 7
1999 9
2000 7
2001 3
2002 6
2003 5
2004 7
2005 3
2006 7
2007 5
2008 5
2009 10
2010 5
2011 1
2012 1
2013 4
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2015 5
2016 4
2017 3
2018 3
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197 results

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Page 1
Single-stranded DNA plasmid, vector construction and cloning of Bacillus stearothermophilus alpha-amylase in Lactobacillus.
Cocconcelli PS, Gasson MJ, Morelli L, Bottazzi V. Cocconcelli PS, et al. Res Microbiol. 1991 Jul-Aug;142(6):643-52. doi: 10.1016/0923-2508(91)90077-n. Res Microbiol. 1991. PMID: 1961976 Free article. Review.
It was shown that the constructed vectors, named pPSC20 and pPSC22, were transformable into L. plantarum, Lactobacillus acidophilus, Lactobacillus reuteri, Lactobacillus fermentum, Lactobacillus helveticus, Lactococcus lactis subsp. lactis, Bacillus subtilis, and Escherich …
It was shown that the constructed vectors, named pPSC20 and pPSC22, were transformable into L. plantarum, Lactobacillus acidophilus, Lactoba …
Enhanced extracellular expression of Bacillus stearothermophilus alpha-amylase in Bacillus subtilis through signal peptide optimization, chaperone overexpression and alpha-amylase mutant selection.
Yao D, Su L, Li N, Wu J. Yao D, et al. Microb Cell Fact. 2019 Apr 11;18(1):69. doi: 10.1186/s12934-019-1119-8. Microb Cell Fact. 2019. PMID: 30971250 Free PMC article.
BACKGROUND: Our laboratory has constructed a Bacillus stearothermophilus alpha-amylase (AmyS) derivative with excellent enzymatic properties. ...RESULTS: In this study, the extracellular production level of B. stearothermophilus alpha- …
BACKGROUND: Our laboratory has constructed a Bacillus stearothermophilus alpha-amylase (AmyS) derivative with ex …
Catalytic properties of maltogenic alpha-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles.
Straksys A, Kochane T, Budriene S. Straksys A, et al. Food Chem. 2016 Nov 15;211:294-9. doi: 10.1016/j.foodchem.2016.05.071. Epub 2016 May 12. Food Chem. 2016. PMID: 27283635
The immobilization of maltogenic alpha-amylase from Bacillus stearothermophilus (BsMa) onto novel porous poly(urethane urea) (PUU) microparticles synthesized from poly(vinyl alcohol) and isophorone diisocyanate was performed by covalent attachment to f …
The immobilization of maltogenic alpha-amylase from Bacillus stearothermophilus (BsMa) onto novel porous poly(ur …
Improving the thermostability and enhancing the Ca(2+) binding of the maltohexaose-forming alpha-amylase from Bacillus stearothermophilus.
Li Z, Duan X, Wu J. Li Z, et al. J Biotechnol. 2016 Mar 20;222:65-72. doi: 10.1016/j.jbiotec.2016.02.013. Epub 2016 Feb 8. J Biotechnol. 2016. PMID: 26869314
The thermostability of the maltohexaose-forming alpha-amylase from Bacillus stearothermophilus (AmyMH) without added Ca(2+) was improved through structure-based rational design in this study. Through comparison of a homologous model structure of AmyMH …
The thermostability of the maltohexaose-forming alpha-amylase from Bacillus stearothermophilus (AmyMH) without a …
Property Improvement of alpha-Amylase fromBacillus stearothermophilus by Deletion of Amino AcidResidues Arginine 179 and Glycine 180.
Gai Y, Chen J, Zhang S, Zhu B, Zhang D. Gai Y, et al. Food Technol Biotechnol. 2018 Mar;56(1):58-64. doi: 10.17113/ftb.56.01.18.5448. Food Technol Biotechnol. 2018. PMID: 29795997 Free PMC article.
To improve the properties of alpha-amylase from Bacillus stearothermophilus (AmyS), a deletion mutant AmySR179-G180 was constructed by deleting arginine (Arg179) and glycine (Gly180) using site-directed mutagenesis. ...In addition, AmySR179-G180 exhibi …
To improve the properties of alpha-amylase from Bacillus stearothermophilus (AmyS), a deletion mutant AmySR179-G …
High-efficiency chromosomal integrative amplification strategy for overexpressing alpha-amylase in Bacillus licheniformis.
Shen P, Niu D, Liu X, Tian K, Permaul K, Singh S, Mchunu NP, Wang Z. Shen P, et al. J Ind Microbiol Biotechnol. 2022 May 25;49(3):kuac009. doi: 10.1093/jimb/kuac009. J Ind Microbiol Biotechnol. 2022. PMID: 35325171 Free PMC article.
Through this procedure, genetically stable recombinants integrated multiple copies of amyS, from Geobacillus stearothermophilus ATCC 31195 were facilely obtained. The genetic stability of the recombinants was verified by repeated subculturing and shaking flask ferme …
Through this procedure, genetically stable recombinants integrated multiple copies of amyS, from Geobacillus stearothermophilus
Efficient Expression of Maltohexaose-Forming alpha-Amylase from Bacillus stearothermophilus in Brevibacillus choshinensis SP3 and Its Use in Maltose Production.
Li Z, Su L, Duan X, Wu D, Wu J. Li Z, et al. Biomed Res Int. 2017;2017:5479762. doi: 10.1155/2017/5479762. Epub 2017 Nov 9. Biomed Res Int. 2017. PMID: 29250543 Free PMC article.
The maltohexaose-forming, Ca(2+)-independent alpha-amylase gene from Bacillus stearothermophilus (AmyMH) was efficiently expressed in Brevibacillus choshinensis SP3. ...Culture medium optimization resulted in an 8-fold improvement in alpha-am
The maltohexaose-forming, Ca(2+)-independent alpha-amylase gene from Bacillus stearothermophilus (AmyMH) was eff …
Expression and Characterization of Geobacillus stearothermophilus SR74 Recombinant alpha-Amylase in Pichia pastoris.
Gandhi S, Salleh AB, Rahman RN, Chor Leow T, Oslan SN. Gandhi S, et al. Biomed Res Int. 2015;2015:529059. doi: 10.1155/2015/529059. Epub 2015 May 18. Biomed Res Int. 2015. PMID: 26090417 Free PMC article.
Geobacillus stearothermophilus SR74 is a locally isolated thermophilic bacteria producing thermostable and thermoactive alpha-amylase. ...The optimum pH of alpha-amylase SR74 was 7.0 and the enzyme was stable between pH 6.0-8.0. ...
Geobacillus stearothermophilus SR74 is a locally isolated thermophilic bacteria producing thermostable and thermoactive alp
Structural and biochemical features of acidic alpha-amylase of Bacillus acidicola.
Sharma A, Satyanarayana T. Sharma A, et al. Int J Biol Macromol. 2013 Oct;61:416-23. doi: 10.1016/j.ijbiomac.2013.08.003. Epub 2013 Aug 13. Int J Biol Macromol. 2013. PMID: 23954129
The investigation is aimed at understanding structure-function aspect of alpha-amylase of an acidophilic bacterium Bacillus acidicola (BAamy), which is Ca(2+)-independent and active at acidic pH of native starch, and thus, suits better in starch saccharificat …
The investigation is aimed at understanding structure-function aspect of alpha-amylase of an acidophilic bacterium Bacillus
197 results