English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

We found here that ω-epoxyalkyl α-D-glucopyranosides consisting of three, four and five alkyl carbons (α-E3G, α-E4G and α-E5G, respectively), which are known to be affinity-labeling reagents of β-amylase, had the effect of inactivating two pullulan-hydrolyzing α-amylases from Thermoactinomyces vulgaris R-47, TVA I and TVA II, at high concentration (ca. 0.1-1.5 M). The inactivation exhibited saturation kinetics of a two-step mechanism, and an inactivation rate constant, k, and equilibrium dissociation constant, KR, of α-E5G were calculated. The k/KR values of α-E5G for TVA I and TVA II were 13.1 × 10-4 and 6.41 × 10-4 M-1 · S-1 respectively. In terms of the power of inactivation, the orders for TVA I and TVA II were α-E5G>α-E3G≈α-E4G, and α-E5G>α-E3G>α-E4G, respectively. The findings indicated that the relation between the lengths of the alkyl carbons and the inactivation of TVA I and TVA II differs from that for β-amylase and isomalto-dextranase.

Inactivation of .ALPHA.-Amylases from Thermoactinomyces vulgaris R-47, TVA I and TVA II, by .OMEGA.-Epoxyalkyl .ALPHA.-D-Glucopyranoside