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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  α–glucosidase (HBGase) plays a key role in hydrolyzing α-glucosidic linkages. In  Apis mellifera , three isoforms of HBGase (I, II and III) have been reported, which differ in their nucleotide composition, encoding amino acid sequences and enzyme kinetics. Recombinant (r)HBGase II from  A. cerana indica  (r Aci HBGase II) was focused upon here due to the fact it is a native and economic honeybee species in Thailand. The data is compared to the two other isoforms,  Aci HBGase I and III from the same bee species and to the three isoforms (HBGase I, II and III) in different bee species where available.    Results  The highest transcript expression level of  AciHBGase II  was found in larvae and pupae, with lower levels in the eggs of  A. cerana indica  but it was not found in foragers. The full-length  AciHBGase II  cDNA, and the predicted amino acid sequence it encodes were 1,740 bp and 579 residues, respectively. The cDNA sequence was 90% identical to that from the HBGase II from the closely related  A. cerana japonica  (GenBank accession # NM_FJ752630.1). The full length cDNA was directionally cloned into the pPICZαA expression vector in frame with a (His) 6  encoding C terminal tag using  Eco RI and  Kpn I compatible ends, and transformed into  Pichia pastoris . Maximal expression of the r Aci HBGase II–(His) 6  protein was induced by 0.5% (v/v) methanol for 96 h and secreted into the culture media. The partially purified enzyme was found to have optimal α-glucosidase activity at pH 3.5 and 45°C, with > 80% activity between pH 3.5–5.0 and 40–55°C, and was stabile (> 80% activity) at pH 4–8 and at < 25–65°C. The optimal substrate was sucrose.    Conclusions  Like in  A. mellifera , there are three isoforms of  Aci HBGase (I, II and III) that differ in their transcript expression pattern, nucleotide sequences and optimal enzyme conditions and kinetics.

Expression of a secretory α-glucosidase II from Apis cerana indica in Pichia pastoris and its characterization