Purification and some properties of the pectin lyase from Penicillium italicum.
For the first time, a pectin lyase (poly(methoxygalacturonide)lyase: EC 4.2.2.10) from a member of the generus Penicillium was isolated, purified to homogeneity and characterized. The monomeric enzyme from Penicillium italicum CECT 2294 culture filtrates showed a molecular mass of 34 kDa after SDS-electrophoresis in polyacrylamide gradient gels, and the isoelectric point was 8.6 as determined by isoelectric focusing. The optimum pH (9.0), the high pH and temperature stabilities, the ability to degrade pectins from different sources and with a wide range of degrees of esterification (from 37% to 86%) as well as the importance of this type of biocatalysts in the food industry make this enzyme an interesting subject of study.
Alaña
A
A
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad del País Vasco/Euskal Herriko Unibertsitatea, Bilbao, Spain.
Lama
M J
MJ
Serra
J L
JL
D000596:Amino Acids / Q000032:analysis; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000302:isolation & purification*; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D011133:Polysaccharide-Lyases; C027349:pectin lyase