Isolation and purification of an acidic pullulanase type II from newly isolated Bacillus sp. US149
A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram +, non-motile, and could grow only in acidic pH (4.5–5.0) between 37 and 55 °C. The strain is likely to be Bacillus naganoensis since the analysis of...
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Published in | Enzyme and microbial technology Vol. 33; no. 5; pp. 720 - 724 |
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Abstract | A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram
+, non-motile, and could grow only in acidic pH (4.5–5.0) between 37 and 55
°C. The strain is likely to be
Bacillus naganoensis since the analysis of the 16S rRNA gene sequence showed highest similarity (96%) with that of
B. naganoensis (accession no.
AB021193). The enzyme was purified to homogeneity by ion exchange and size exclusion chromatography from cell free culture supernatant. The purified native form had an estimated molecular mass of 200
kDa and it is composed of two subunits each of 95
kDa determined by SDS–PAGE. The purified enzyme had an optimum pH of 5 and retained activity at pH lower than 5. It had half-life duration of 48 and 20
min at 80 and 90
°C, respectively. The enzyme could hydrolyze pullulan, but it was unable to hydrolyze amylose and maltoheptaose. It was demonstrated that the DP3 product of pullulan hydrolysis was isopanose since it was cleaved by α-glucosidase to form glucose and isomaltose. This proved that the PulUS149 is an isopullulanase (pullulan-4-glucanohydrolase, EC 3.2.1.57) classified under pullulanase type II. |
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AbstractList | A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram
+, non-motile, and could grow only in acidic pH (4.5–5.0) between 37 and 55
°C. The strain is likely to be
Bacillus naganoensis since the analysis of the 16S rRNA gene sequence showed highest similarity (96%) with that of
B. naganoensis (accession no.
AB021193). The enzyme was purified to homogeneity by ion exchange and size exclusion chromatography from cell free culture supernatant. The purified native form had an estimated molecular mass of 200
kDa and it is composed of two subunits each of 95
kDa determined by SDS–PAGE. The purified enzyme had an optimum pH of 5 and retained activity at pH lower than 5. It had half-life duration of 48 and 20
min at 80 and 90
°C, respectively. The enzyme could hydrolyze pullulan, but it was unable to hydrolyze amylose and maltoheptaose. It was demonstrated that the DP3 product of pullulan hydrolysis was isopanose since it was cleaved by α-glucosidase to form glucose and isomaltose. This proved that the PulUS149 is an isopullulanase (pullulan-4-glucanohydrolase, EC 3.2.1.57) classified under pullulanase type II. A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram super(+), non-motile, and could grow only in acidic pH (4.5-5.0) between 37 and 55 degree C. The strain is likely to be Bacillus naganoensis since the analysis of the 16S rRNA gene sequence showed highest similarity (96%) with that of B. naganoensis (accession no. AB021193). The enzyme was purified to homogeneity by ion exchange and size exclusion chromatography from cell free culture supernatant. The purified native form had an estimated molecular mass of 200 kDa and it is composed of two subunits each of 95 kDa determined by SDS-PAGE. The purified enzyme had an optimum pH of 5 and retained activity at pH lower than 5. It had half-life duration of 48 and 20 min at 80 and 90 degree C, respectively. The enzyme could hydrolyze pullulan, but it was unable to hydrolyze amylose and maltoheptaose. It was demonstrated that the DP3 product of pullulan hydrolysis was isopanose since it was cleaved by alpha -glucosidase to form glucose and isomaltose. This proved that the PulUS149 is an isopullulanase (pullulan-4- glucanohydrolase, EC 3.2.1.57) classified under pullulanase type II. |
Author | Messaoud, E.Ben Roy, Amitava Bejar, S. |
Author_xml | – sequence: 1 givenname: Amitava surname: Roy fullname: Roy, Amitava – sequence: 2 givenname: E.Ben surname: Messaoud fullname: Messaoud, E.Ben – sequence: 3 givenname: S. surname: Bejar fullname: Bejar, S. email: Samir.bejar@cbs.rnrt.tn |
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Cites_doi | 10.1042/bj3230859 10.1021/ac60147a030 10.1080/00021369.1971.10860023 10.1128/aem.63.3.1088-1094.1997 10.1099/00207713-40-2-123 10.1128/JB.182.22.6331-6338.2000 10.1016/S0141-0229(02)00185-0 10.1271/bbb.60.1795 10.1023/A:1010597619811 10.1128/aem.61.2.567-575.1995 10.1128/jb.171.1.369-374.1989 10.1099/13500872-142-1-3 10.1007/BF00127894 10.1073/pnas.74.12.5463 10.1042/bj3230757 10.2323/jgam.46.1 10.1128/AEM.65.5.2084-2091.1999 10.1128/AEM.65.4.1644-1651.1999 10.1128/aem.63.9.3577-3584.1997 10.1038/227680a0 |
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Microbiol. doi: 10.1128/AEM.65.4.1644-1651.1999 contributor: fullname: Kim – ident: 10.1016/S0141-0229(03)00212-6_BIB16 – volume: 63 start-page: 3577 year: 1997 ident: 10.1016/S0141-0229(03)00212-6_BIB7 article-title: Cloning, sequencing and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme publication-title: Appl. Environ. Microbiol. doi: 10.1128/aem.63.9.3577-3584.1997 contributor: fullname: Dong – volume: 227 start-page: 680 year: 1970 ident: 10.1016/S0141-0229(03)00212-6_BIB18 article-title: Cleavage of structure protein during assembly of head of bacteriophage T4 publication-title: Nature doi: 10.1038/227680a0 contributor: fullname: Laemmeli |
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Snippet | A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram
+,... A strain US149 having high pullulanase activity was isolated from Tunisian soil adjacent to hot spring. The cells of this strain were rod shaped, Gram... |
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SubjectTerms | 16S rRNA a-dextrin endo-1,6-a-glucosidase Bacillus Bacillus naganoensis Isopullulanase Protein purification pullulan pullulan-4-glucanohydrolase |
Title | Isolation and purification of an acidic pullulanase type II from newly isolated Bacillus sp. US149 |
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