## Abstract Acidic alpha‐D‐mannosidase purified from the hepatopancreas of __Penaeus monodon__ is pentameric, with a Mr 251,000 as estimated by size‐exclusion FPLC on a Superose^TM^ 12, and retains a hydrophobic domain, being stable to heating at 65°C for 1 h. The specific activity of the purified
Alpha-glucosidase from the hepatopancreas of the shrimp,Penaus vannamei (Crustacea-Decapoda)
✍ Scribed by Le Chevalier, Patrick; Van Wormhoudt, Alain
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 499 KB
- Volume
- 280
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
✦ Synopsis
Penaeus vannamei is an omnivorous species, and it can be assumed that a high level of carbohydrates is necessary for growth. Alpha-glucosidases are important enzymes necessary for the ultimate liberation of glucose residues from various carbohydrates. Using acarbose affinity chromatography, a glycosylated alpha-glucosidase with a molecular mass of approximately 105 kDa was isolated for the first time from the hepatopancreas of the shrimp. Exhibiting an optimal catalytic activity in the temperature range from 40°C to 50°C at pH 6, the purified enzyme hydrolyses α 1-4 bonds and liberates glucose from different oligo and polysaccharides. By contrast to other known glucosidases, no α 1-6 glucose link with hydrolysis has been observed. This could explain the different rates of growth in shrimp aquaculture with starches from various origins. The amino-acid composition, together with the partial sequence of a hydrolytic peptide, shows a high degree of similarity to the alpha-glucosidases reported for various organisms including yeast and fungi and may help determine the phylogeny of the family.
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