Abstract
The molecular properties, such as molecular weight, N-and C-terminal amino acids, amino acid composition, and circular dichroism, of 1,2-α-mannosidase isolated from the culture filtrate ofAspergillus saitoi were determined.
The enzyme had aK m of 0.67 mM andk cat of 1.27/s with mannobiose at pH 50.0 and 30°C. The anomeric configuration of the reaction products of the enzyme was examined by studying the α-anomer. A single Manαl→2Man linkage in intact Taka-amylase A fromAspergillus oryzae was hydrolyzed, producing free mannose.
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Shigematsu, Y., Tsukahara, K., Tanaka, T. et al. Molecular and enzymatic properties of 1,2-α-d-mannosidase fromAspergillus saitoi . Current Microbiology 13, 43–46 (1986). https://doi.org/10.1007/BF01568158
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DOI: https://doi.org/10.1007/BF01568158