Heterologous expression and characterization of class III chitinases from rice (Oryza sativa L.)

Seung Moon Park; Dae Hyuk Kim; Nam Hai Truong; Yoshifumi Itoh

doi:10.1016/S0141-0229(02)00042-X

Heterologous expression and characterization of class III chitinases from rice (Oryza sativa L.)

Seung Moon Park^*
, Dae Hyuk Kim
, Nam Hai Truong
, Yoshifumi Itoh

^*Corresponding author for this work

National Agriculture and Food Research Organization

Research output: Contribution to journal › Journal article › peer-review

21 Scopus citations

Abstract

Acidic (OsChib1a) and basic (OsChib1b) class III chitinases from rice (Oryza sativa L.), sharing 70% of the identical amino acid residues each other, were expressed from the corresponding cDNAs in Pichia pastoris and purified homogenously. Both OsChib1a and OsChib1b degraded actively glycol chitin over colloidal chitin at the optimum pH of 4.3 and 8.3, respectively. OsChib1b had lower specific chitinase activity than OsChib1a, but it showed a strong lytic activity and significant antifungal activity: no lytic and antifungal activity was observed for OsChib1a. Experiments with N-acetyl chitooligosaccharides showed that OsChib1a hydrolyzed (GlcNAc)₆ efficiently to yield (GlcNAc)₂ as the major product, while OsChib1b hydrolyzed (GlcNAc)₆ to yield both (GlcNAc)₂ and (GlcNAc)₄. Possible structures responsible for their distinct catalytic properties are discussed.

Original language	English
Pages (from-to)	697-702
Number of pages	6
Journal	Enzyme and Microbial Technology
Volume	30
Issue number	6
DOIs	https://doi.org/10.1016/S0141-0229(02)00042-X
State	Published - 2002.05.27

Keywords

Class III Chitinase
N-acetylchitooligosaccharide
Oryza sativa L.
Pathogenesis related protein
Pichia pastoris

Quacquarelli Symonds(QS) Subject Topics

Engineering - Chemical
Biological Sciences

Access to Document

10.1016/S0141-0229(02)00042-X

Cite this

@article{9fba2b8f286c420a957f8c8b88ddc85f,

title = "Heterologous expression and characterization of class III chitinases from rice (Oryza sativa L.)",

abstract = "Acidic (OsChib1a) and basic (OsChib1b) class III chitinases from rice (Oryza sativa L.), sharing 70\% of the identical amino acid residues each other, were expressed from the corresponding cDNAs in Pichia pastoris and purified homogenously. Both OsChib1a and OsChib1b degraded actively glycol chitin over colloidal chitin at the optimum pH of 4.3 and 8.3, respectively. OsChib1b had lower specific chitinase activity than OsChib1a, but it showed a strong lytic activity and significant antifungal activity: no lytic and antifungal activity was observed for OsChib1a. Experiments with N-acetyl chitooligosaccharides showed that OsChib1a hydrolyzed (GlcNAc)6 efficiently to yield (GlcNAc)2 as the major product, while OsChib1b hydrolyzed (GlcNAc)6 to yield both (GlcNAc)2 and (GlcNAc)4. Possible structures responsible for their distinct catalytic properties are discussed.",

keywords = "Class III Chitinase, N-acetylchitooligosaccharide, Oryza sativa L., Pathogenesis related protein, Pichia pastoris",

author = "Park, \{Seung Moon\} and Kim, \{Dae Hyuk\} and Truong, \{Nam Hai\} and Yoshifumi Itoh",

year = "2002",

month = may,

day = "27",

doi = "10.1016/S0141-0229(02)00042-X",

language = "English",

volume = "30",

pages = "697--702",

journal = "Enzyme and Microbial Technology",

issn = "0141-0229",

number = "6",

}

TY - JOUR

T1 - Heterologous expression and characterization of class III chitinases from rice (Oryza sativa L.)

AU - Park, Seung Moon

AU - Kim, Dae Hyuk

AU - Truong, Nam Hai

AU - Itoh, Yoshifumi

PY - 2002/5/27

Y1 - 2002/5/27

N2 - Acidic (OsChib1a) and basic (OsChib1b) class III chitinases from rice (Oryza sativa L.), sharing 70% of the identical amino acid residues each other, were expressed from the corresponding cDNAs in Pichia pastoris and purified homogenously. Both OsChib1a and OsChib1b degraded actively glycol chitin over colloidal chitin at the optimum pH of 4.3 and 8.3, respectively. OsChib1b had lower specific chitinase activity than OsChib1a, but it showed a strong lytic activity and significant antifungal activity: no lytic and antifungal activity was observed for OsChib1a. Experiments with N-acetyl chitooligosaccharides showed that OsChib1a hydrolyzed (GlcNAc)6 efficiently to yield (GlcNAc)2 as the major product, while OsChib1b hydrolyzed (GlcNAc)6 to yield both (GlcNAc)2 and (GlcNAc)4. Possible structures responsible for their distinct catalytic properties are discussed.

AB - Acidic (OsChib1a) and basic (OsChib1b) class III chitinases from rice (Oryza sativa L.), sharing 70% of the identical amino acid residues each other, were expressed from the corresponding cDNAs in Pichia pastoris and purified homogenously. Both OsChib1a and OsChib1b degraded actively glycol chitin over colloidal chitin at the optimum pH of 4.3 and 8.3, respectively. OsChib1b had lower specific chitinase activity than OsChib1a, but it showed a strong lytic activity and significant antifungal activity: no lytic and antifungal activity was observed for OsChib1a. Experiments with N-acetyl chitooligosaccharides showed that OsChib1a hydrolyzed (GlcNAc)6 efficiently to yield (GlcNAc)2 as the major product, while OsChib1b hydrolyzed (GlcNAc)6 to yield both (GlcNAc)2 and (GlcNAc)4. Possible structures responsible for their distinct catalytic properties are discussed.

KW - Class III Chitinase

KW - N-acetylchitooligosaccharide

KW - Oryza sativa L.

KW - Pathogenesis related protein

KW - Pichia pastoris

UR - https://www.scopus.com/pages/publications/0037182335

U2 - 10.1016/S0141-0229(02)00042-X

DO - 10.1016/S0141-0229(02)00042-X

M3 - Journal article

AN - SCOPUS:0037182335

SN - 0141-0229

VL - 30

SP - 697

EP - 702

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 6

ER -

Heterologous expression and characterization of class III chitinases from rice (Oryza sativa L.)

Abstract

Keywords

Quacquarelli Symonds(QS) Subject Topics

Access to Document

Other files and links

Fingerprint

Cite this