Abstract
The β-glucosidase of apricot seeds was purified to a preparation contain a negligible trace amount of α-amylase.
The crystalline β-amylase hydrolyzed amylose to a limit at 73.4% as maltose, so the existence of the arrest point to the β-amylolysis was confirmed.
The purified β-glucosidase could not supplement the crystalline β-amylase, on the hydrolysis of amylose limit β-dextrin.
Hence it may here be considered that the presence of a β-glucosidase-labile linkage in amylose as described by Peat et al., is not convincible.
