Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125
Production of β-xylosidaseby a cycloheximide and 2-deoxy-D-glucose-resistant mutant of Kluyveromyces marxianus PPY125 was studied when cultured on growth media containing galactose, glucose, xylose, cellobiose, sucrose and lactose as carbon sources. Xylose, cellobiose, lactose and sucrose w...
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Pontificia Universidad Católica de Valparaíso
2005
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oai:scielo:S0717-345820050002000072005-10-14Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125Rajoka,Muhammad IbrahimKhan,Sana enthalpy entropy enzyme kinetics fermentation induction thermodynamics Production of β-xylosidaseby a cycloheximide and 2-deoxy-D-glucose-resistant mutant of Kluyveromyces marxianus PPY125 was studied when cultured on growth media containing galactose, glucose, xylose, cellobiose, sucrose and lactose as carbon sources. Xylose, cellobiose, lactose and sucrose were the key substrates. Both K. marxianus PPY125 and its mutant (M 125) supported maximum β-xylosidase specific product yield (Y P/X) following growth on xylose. Basal level of activity was observed in non-induced cultures grown on glucose. The mutant produced 1.5 to 2-fold more β-xylosidase than that produced by the wild cells. Synthesis of β-xylosidase was regulated by an induction mechanism in both wild and mutant cells. Addition of glucose did not inhibit the synthesis of β-xylosidase in both parental and mutant cultures in the presence of corn steep liquor. Partially purified enzyme showed good stability when incubated at 60ΊC and was quite stable at pH 5.0-7.0. Thermodynamic studies revealed that the enzyme derived by the mutant M125 was more thermostable as evidenced by higher midpoint inactivation temperature, lower activation energy demand for β-xyloside hydrolysis, as well as lower enthalpy and entropy demand for reversible denaturation of enzymeinfo:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.8 n.2 20052005-08-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582005000200007en |
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Scielo Chile |
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Scielo Chile |
| language |
English |
| topic |
enthalpy entropy enzyme kinetics fermentation induction thermodynamics |
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enthalpy entropy enzyme kinetics fermentation induction thermodynamics Rajoka,Muhammad Ibrahim Khan,Sana Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| description |
Production of β-xylosidaseby a cycloheximide and 2-deoxy-D-glucose-resistant mutant of Kluyveromyces marxianus PPY125 was studied when cultured on growth media containing galactose, glucose, xylose, cellobiose, sucrose and lactose as carbon sources. Xylose, cellobiose, lactose and sucrose were the key substrates. Both K. marxianus PPY125 and its mutant (M 125) supported maximum β-xylosidase specific product yield (Y P/X) following growth on xylose. Basal level of activity was observed in non-induced cultures grown on glucose. The mutant produced 1.5 to 2-fold more β-xylosidase than that produced by the wild cells. Synthesis of β-xylosidase was regulated by an induction mechanism in both wild and mutant cells. Addition of glucose did not inhibit the synthesis of β-xylosidase in both parental and mutant cultures in the presence of corn steep liquor. Partially purified enzyme showed good stability when incubated at 60ΊC and was quite stable at pH 5.0-7.0. Thermodynamic studies revealed that the enzyme derived by the mutant M125 was more thermostable as evidenced by higher midpoint inactivation temperature, lower activation energy demand for β-xyloside hydrolysis, as well as lower enthalpy and entropy demand for reversible denaturation of enzyme |
| author |
Rajoka,Muhammad Ibrahim Khan,Sana |
| author_facet |
Rajoka,Muhammad Ibrahim Khan,Sana |
| author_sort |
Rajoka,Muhammad Ibrahim |
| title |
Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| title_short |
Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| title_full |
Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| title_fullStr |
Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| title_full_unstemmed |
Hyper-production of a thermotolerant β-xylosidase by a deoxy-D-glucose and cycloheximide resistant mutant derivative of Kluyveromyces marxianus PPY 125 |
| title_sort |
hyper-production of a thermotolerant β-xylosidase by a deoxy-d-glucose and cycloheximide resistant mutant derivative of kluyveromyces marxianus ppy 125 |
| publisher |
Pontificia Universidad Católica de Valparaíso |
| publishDate |
2005 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582005000200007 |
| work_keys_str_mv |
AT rajokamuhammadibrahim hyperproductionofathermotolerant946xylosidasebyadeoxydglucoseandcycloheximideresistantmutantderivativeofkluyveromycesmarxianusppy125 AT khansana hyperproductionofathermotolerant946xylosidasebyadeoxydglucoseandcycloheximideresistantmutantderivativeofkluyveromycesmarxianusppy125 |
| _version_ |
1718441733852758016 |