Purification and properties of a beta-mannosidase from shrimp (Penaeus japonicus) hepatopancreas.
作者： Nin-Nin Chuang , Bei-Chia Yang
DOI: 10.1016/0305-0491(91)90266-G
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摘要: Abstract 1. A β-mannosidase was purified ca 720-fold to homogeneity from Penaeus japonicus, with a final spec. act. of 252 U/mg protein. 2. By using SDS-polyacrylamide gel electrophoresis, the monomers shrimp were discovered have mol. wts 31,000 and those human placental enzyme similar wts. 3. The has an isoelectric point (pI) 5.6 ± 0.1, identical pI. Both enzymes sialyated. 4. pH optimum at 5.0 its Km 123 μM 4-methylumbelliferyl-β- d -mannopyranoside as substrate. 4.5 10 μM. 5. In contrast discovery thermostability β-mannosidase, found be labile heating 45°C for 20 min. activities inhibited by Hg2+ Cd2+ ions. However, is significantly more sensitive inhibition.
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