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Effect of partial deglycosylation on catalytic characteristics and stability of an avocado peroxidase
Author(s) -
SánchezRomero Carolina,
GarcíaGómez María L.,
PliegoAlfaro Fernando,
Heredia Antonio
Publication year - 1994
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1994.tb06660.x
Subject(s) - persea , glycosidic bond , chemistry , moiety , peroxidase , enzyme , acetic acid , biochemistry , stereochemistry , chromatography , botany , biology
An isoperoxidase (EC 1.11.1.7) purified from avocado ( Persea americana Mill. cv. Topa Topa) leaves, lost 35% of its glycosidic moiety after incubation with glycopeptidase F (EC 3.2.2.18). The partial removal of carbohydrate chains caused a decrease in the K m for reductor substrates tguaiacol, syringaldazine and indole‐3‐acetic acid) and favoured the enzyme activation by Ca 2+ . A decrease in stability against temperature was also observed. Our results are consistent with the hypothesis that the carbohydrate moiety located on the surface of the peroxidase molecule acts as a molecular shield.