Purification and characterization of an anionic isoperoxidase from scented-geranium callus SCIE SCOPUS

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Title
Purification and characterization of an anionic isoperoxidase from scented-geranium callus
Author(s)
Min, BS; Kim, YK; Ma, CW; Jin, ES; Lee, TK; Lee, JK; Lee, YB; Ryoo, KK; Lee, MY
KIOST Author(s)
Lee, Taek Kyun(이택견)
Publication Year
2004
Abstract
Secretory anionic isoperoxidase (EC 1.11.1.7), named PA1, was 68-fold purified from scented-geranium (Pelargonium graveolense) callus by using ion exchange chromatography and gel filtration. Isoperoxidase PA1 was a glycoprotein with an isoelectric point (pI) of 4.0. The molecular weight of PA1 was approximately 42.5 and 44 kDa, estimated by SDS PAGE and Sephadex G-150 gel filtration, respectively. The optimum pH of the enzyme was 5.0 for guaiacol and H2O2, and the K-m values for guaiacol and H2O2 were 1.96 and 8.5 mM, respectively. Substrate studies in terms of optimum pHs and K-m values with various synthetic and naturally occurring phenolic compounds were performed. In comparison with cationic isoperoxidase, PC3, which has been already characterized, anionic isoperoxidase PA1 had much lower K-m values for synthetic phenolic compounds and much higher K-m values for naturally occurring phenolic compounds than PC3. Moreover, anionic isoperoxidase PA1 could utilize ferulic acid as a substrate very well, while cationic isoperoxidase PC3 could not utilize ferulic acid as a substrate.
ISSN
1082-6068
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/5364
DOI
10.1081/PB-200026809
Bibliographic Citation
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, v.34, no.3, pp.253 - 264, 2004
Publisher
TAYLOR & FRANCIS INC
Subject
LIGNIN PEROXIDASE; STREPTOMYCES-VIRIDOSPORUS; RADISH; CONVERSION; REMOVAL; ACID
Keywords
anionic isoperoxidase; Pelargonium graveolens; purification; characterization
Type
Article
Language
English
Document Type
Article
Publisher
TAYLOR & FRANCIS INC
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