<abstract xmlns="http://www.w3.org/1999/xhtml"> A bacterial strain was isolated from Pasinler hot spring, Erzurum, Turkey. The purified thermophilic isolate was identified as Geobacillus pallidus P26 and used to produce extracellular pectin lyase (EC 4.2.2.10). Pectin lyase enzyme was purified 34 fold by using DEAE-cellulose anion exchange column chromatography and characterized. Molecular weight of the enzyme was determined as 56 kDa by using Sephadex G-100 gel filtration chromatography. Purification of enzyme was verified by SDS-PAGE. The pH- and temperature optima of enzyme were determined (pH 9.0 and 60°C, respectively). Pectin lyase was mostly stable at 50 oC for 24 hours. Its’ activity decreased to 50 % for 24 h at 60°C. KM and Vmax were calculated as 24.8 mg/mL and 2.28 μmol/L min, respectively. Purified pectin lyase was inhibited by Fe3+, Zn2+, Cu2+, Ca2+, Co2+ and Hg2+ but not by Mg2+. The purified pectin lyase enzyme was used for getting fruits juices. It was found that yields of fruits juices increased when they were compared with control.</abstract>

A bacterial strain was isolated from Pasinler hot spring, Erzurum, Turkey. The purified thermophilic isolate was identified as Geobacillus pallidus P26 and used to produce extracellular pectin lyase (EC 4.2.2.10). Pectin lyase enzyme was purified 34 fold by using DEAE-cellulose anion exchange column chromatography and characterized. Molecular weight of the enzyme was determined as 56 kDa by using Sephadex G-100 gel filtration chromatography. Purification of enzyme was verified by SDS-PAGE. The pH- and temperature optima of enzyme were determined (pH 9.0 and 60°C, respectively). Pectin lyase was mostly stable at 50 oC for 24 hours. Its’ activity decreased to 50 % for 24 h at 60°C. KM and Vmax were calculated as 24.8 mg/mL and 2.28 μmol/L min, respectively. Purified pectin lyase was inhibited by Fe3+, Zn2+, Cu2+, Ca2+, Co2+ and Hg2+ but not by Mg2+. The purified pectin lyase enzyme was used for getting fruits juices. It was found that yields of fruits juices increased when they were compared with control.

Production of pectin lyase from Geobacillus pallidus p26, purification, characterization and fruit juice application

College of Education, Bayburt University, 69000, Bayburt, Turkey

College of Art and Science, Muğla University, 48000, Muğla, Turkey

Atatürk University, Faculty of Science, Molecular Biology and Genetics Department, 25240, Erzurum, Turkey

Atatürk University, Faculty of Science, Biology Department, 25240, Erzurum, Turkey

Acta Chimica Slovaca

This article is distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

A bacterial strain was isolated from Pasinler hot spring, Erzurum, Turkey. The purified thermophilic isolate was identified as Geobacillus pallidus P26 and...

Production of pectin lyase from Geobacillus pallidus p26, purification, characterization and fruit juice application

Publicado en línea: 27 may 2014

Páginas: 57 - 63

DOI: https://doi.org/10.2478/acs-2014-0011

Palabras clave
Pectin lyase, purification, characterization, Geobacillus pallidus P26

© Faculty of Chemical and Food Technology, Slovak University of Technology in Bratislava

This article is distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Production of pectin lyase from Geobacillus pallidus p26, purification, characterization and fruit juice application

Publicado en línea: 27 may 2014

Páginas: 57 - 63

DOI: https://doi.org/10.2478/acs-2014-0011

Palabras clavePectin lyase, purification, characterization, Geobacillus pallidus P26

© Faculty of Chemical and Food Technology, Slovak University of Technology in Bratislava

This article is distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Palabras clave
Pectin lyase, purification, characterization, Geobacillus pallidus P26