Heterologous expression of the Saccharomyces cerevisiae PGU1 gene in Schizosaccharomyces pombe yields an enzyme with more desirable properties for the food industry.
The Saccharomyces cerevisiae PGU1 gene was successfully expressed in Schizosaccharomyces pombe. The optimum pH and temperature for the recombinant enzyme were 5 and 40 degrees C, respectively, these being around 0.5 U higher and 5 degrees C lower than those shown by the native enzyme. The K(m) value was about fourfold higher than that of the S. cerevisiae enzyme. The recombinant endopolygalacturonase was more efficient in reducing the viscosity of polygalacturonic acid and was also more stable at different pHs and temperatures than the native enzyme.
Sieiro
C
C
Department of Microbiology, Faculty of Pharmacy, University of Santiago de Compostela, 15782 Santiago de Compostela, Spain.
Poza
M
M
Vilanova
M
M
Villa
T G
TG
D003470:Culture Media; D019649:Food Industry; D006863:Hydrogen-Ion Concentration; D010368:Pectins / Q000378:metabolism; D011096:Polygalacturonase / Q000096:biosynthesis* / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D012568:Schizosaccharomyces / Q000201:enzymology / Q000235:genetics*; D013696:Temperature; D014783:Viscosity
D003470:Culture Media; D011994:Recombinant Proteins; D010368:Pectins; D011096:Polygalacturonase; C003181:polygalacturonic acid