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Purification and substrate specificity of peroxidase from sweet potato tubers

Castillo Leon, Jaime LU ; Alpeeva, I S; Chubar, T A; Galaev, Igor LU ; Csöregi, Elisabeth LU and Sakharov, I Y (2002) In Plant Science 163(5). p.1011-1019
Abstract
Previously the screening of tropical plants demonstrated a high peroxidase activity in sweet potato (Ipomoea batatas) tubers. The major peroxidase pool is localized in peel. Using peel of sweet potato as a source, the sweet potato peroxidase (SPP) has been isolated and purified to homogeneity. The enzyme purification included homogenization, extraction of colored compounds and consecutive chromatographies on Phenyl-Sepharose and DEAE-Toyopearl. The purified SPP had specific activity of 4900 U mg(-1) protein, RZ (ratio of absorbances at 403 and 280 nm, respectively) 3.4, molecular mass of 37 kDa and isoelectric point of 3.5. The spectrum of peroxidase from sweet potato is typical for plant peroxidases with a Soret maximum at 401 nm and the... (More)
Previously the screening of tropical plants demonstrated a high peroxidase activity in sweet potato (Ipomoea batatas) tubers. The major peroxidase pool is localized in peel. Using peel of sweet potato as a source, the sweet potato peroxidase (SPP) has been isolated and purified to homogeneity. The enzyme purification included homogenization, extraction of colored compounds and consecutive chromatographies on Phenyl-Sepharose and DEAE-Toyopearl. The purified SPP had specific activity of 4900 U mg(-1) protein, RZ (ratio of absorbances at 403 and 280 nm, respectively) 3.4, molecular mass of 37 kDa and isoelectric point of 3.5. The spectrum of peroxidase from sweet potato is typical for plant peroxidases with a Soret maximum at 401 nm and the maxima in the visible region at 497 and 638 nm, respectively. The substrate specificity of SPP is distinct from the specificity of other plant peroxidases, ferulic acid being the best substrate for SPP. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
substrate specificity, purification, peroxidase, sweet potato
in
Plant Science
volume
163
issue
5
pages
1011 - 1019
publisher
Elsevier
external identifiers
  • wos:000179717900010
  • scopus:0036852851
ISSN
0168-9452
DOI
10.1016/S0168-9452(02)00275-3
language
English
LU publication?
yes
id
49f620df-f9d1-4bea-bc67-5b7bd430b370 (old id 321494)
date added to LUP
2007-11-14 13:23:17
date last changed
2017-10-01 04:47:38
@article{49f620df-f9d1-4bea-bc67-5b7bd430b370,
  abstract     = {Previously the screening of tropical plants demonstrated a high peroxidase activity in sweet potato (Ipomoea batatas) tubers. The major peroxidase pool is localized in peel. Using peel of sweet potato as a source, the sweet potato peroxidase (SPP) has been isolated and purified to homogeneity. The enzyme purification included homogenization, extraction of colored compounds and consecutive chromatographies on Phenyl-Sepharose and DEAE-Toyopearl. The purified SPP had specific activity of 4900 U mg(-1) protein, RZ (ratio of absorbances at 403 and 280 nm, respectively) 3.4, molecular mass of 37 kDa and isoelectric point of 3.5. The spectrum of peroxidase from sweet potato is typical for plant peroxidases with a Soret maximum at 401 nm and the maxima in the visible region at 497 and 638 nm, respectively. The substrate specificity of SPP is distinct from the specificity of other plant peroxidases, ferulic acid being the best substrate for SPP.},
  author       = {Castillo Leon, Jaime and Alpeeva, I S and Chubar, T A and Galaev, Igor and Csöregi, Elisabeth and Sakharov, I Y},
  issn         = {0168-9452},
  keyword      = {substrate specificity,purification,peroxidase,sweet potato},
  language     = {eng},
  number       = {5},
  pages        = {1011--1019},
  publisher    = {Elsevier},
  series       = {Plant Science},
  title        = {Purification and substrate specificity of peroxidase from sweet potato tubers},
  url          = {http://dx.doi.org/10.1016/S0168-9452(02)00275-3},
  volume       = {163},
  year         = {2002},
}