Open AccessPurification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger
Author(s) -
Kester Harry C.M.,
Visser Jaap
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07008.x
Subject(s) - aspergillus niger , pectin , pectin lyase , enzyme , biochemistry , molecular mass , extracellular , pectinesterase , biology , chemistry , pectinase
An Aspergillus niger multicopy pki‐pel B fusion transformant was used to overexpress pectin lyase B. Under the control of this glycolytic promoter no other contaminating extracellular pectinolytic enzymes appeared in the culture fluid. PL B could thus be purified easily. It has a molecular mass of 40 kDa and has been characterizd as an endo‐acting enzyme. The iso‐electric point of PL B (5.9) is much higher than the pI‐values of two other A. niger pectin lyases viz. pI 3.65 for PL I and pI 3.75 for PL II). Other differences between this enzyme and the two other well characterized pectin lyases are the much higher pH optimum and the higher turnover number on highly esterified pectin for PL B.