Synthesis, (1→3)‐β‐D‐Glucanase‐Binding Ability and Phytoalexin‐Elicitor Activity of (R)‐2,3‐Epoxypropyl (1→3)‐β‐D‐Pentaglucoside.

Huang, Gangliang; Mei, Xiaoguang; Liu, Manxi; Liu, Tiancai

doi:10.1002/chin.200515184

Search citation statements

Order By: Relevance

Paper Sections

Select...

Binding Chitinase Assay1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2007

Publication Types

Select...

Article1

Relationship

Self Cite1

Independent0

Authors

Journals

Cited by 1 publication

(1 citation statement)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, we also assayed the inactivating ability of 3 and 4 towards the chitinase from Serratia marcescens. The chitinase activity was measured by determining the amount of reducing sugar equivalents released on incubation of the enzyme with the substrate p-nitrophenyl N-acetyl-b-D-glucosaminide under the condition stated [6][7]. The inhibition constants (k i ) found for 3 and 4 were 13.9 mmol/L and 55.3 mmol/L, respectively, so that, 4 is much more stable than 3.…”

Section: Binding Chitinase Assaymentioning

confidence: 99%

Production and chitinase-binding ability of lipo-chitopentaose nodulation factor

Huang

Mei

2007

Journal of Enzyme Inhibition and Medicinal Chemistry

Self Cite

View full text Add to dashboard Cite

The penta-N-acetyl-chitopentaose 2 has been prepared by using recombinant E. coli strains harboring the nodC gene (encoding chitooligosaccharide synthase) from Azorhizobium caulinodans. Then, the deacetylase NodB removed the N-acetyl moiety from the nonreducing terminus of 2 to give tetra-N-acetyl-chitopentaose 3. N-Acylation of 3 with stearyl chloride was performed in DMF containing water and provided the corresponding lipo-chitopentaose nodulation factor 4. A binding chitinase assay indicated that 4 was much more stable than 3.

show abstract

Section: Binding Chitinase Assaymentioning

confidence: 99%