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Ryu Hwa-Ja Seo Eun-Seong Kang Hee-Kyoung Kim Young-Min Kim Doman 《Food science and biotechnology》2011,20(2):561-565
A gene encoding human intestinal maltase (HMA) was successfully expressed in Pichia pastoris under the control of the methanol-induced alcohol oxidase (AOX1) promoter. The secreted recombinant HMA fused with a His6-tag was produced (150 U/L) and was easily purified from culture supernatants in a 3-step diafiltration, ultrafiltration,
and affinity column chromatography protocol. The specific activity of the purified HMA was 16.8 U/mg. Endoglycosidase H digestion
of the protein showed that the recombinant HMA was N-glycosylated. The purified HMA was maximally active at pH 6.5 and stable (≥90%) up to 65°C. The kinetic parameters K
m
and V
max
were 3.3±0.25 mM maltose and 61.9±2 U/mg, respectively. 相似文献
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