Characterization of an acidic pectin methylesterase from Paenibacillus xylanexedens and its application in fruit processing.
Protein Expr Purif
; 179: 105798, 2021 03.
Article
in En
| MEDLINE
| ID: mdl-33232801
ABSTRACT
A pectinase-producing bacterial isolate, identified as Paenibacillus xylanexedens SZ 29, was screened by using the soil dilution plate with citrus pectin and congo red. A pectin methylesterase gene (Pxpme) was cloned and expressed in Escherichia coli. The gene coded for a protein with 334 amino acids and a calculated molecular mass of 36.76 kDa. PxPME showed the highest identity of 32.4% with the characterized carbohydrate esterase family 8 pectin methylesterase from Daucus carota. The recombined PxPME showed a specific activity with 39.38 U/mg against citrus pectin with >65% methylesterification. The optimal pH and temperature for PxPME activity were 5.0 and 45 °C. Its Km and Vmax value were determined to be 1.43 mg/mL and 71.5 µmol/mg·min, respectively. Moreover, PxPME could increase the firmness of pineapple cubes by 114% when combined with CaCl2. The acidic and mesophilic properties make PxPME a potential candidate for application in the fruit processing.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Recombinant Proteins
/
Carboxylic Ester Hydrolases
/
Pectins
/
Paenibacillus
Language:
En
Journal:
Protein Expr Purif
Year:
2021
Type:
Article
Affiliation country:
China