α-Galactosidases are broadly used in feed, food, chemical, pulp, and pharmaceutical industries. However, there lacks a satisfactory microbial cell factory that is able to produce α-galactosidases efficiently and cost-effectively to date, which prevents these important enzymes from greater application. In this study, the secretory expression of an Aspergillus niger α-galactosidase (AGA) in Pichi...

1. A previously uncharacterized form of human liver acid ,B-galactosidase (EC 3.2.1.23), possibly a dimer of molecular weight 160000, was resolved by gel filtration. It has the same ability to hydrolyse GM, ganglioside as the two other acid ,B-galactosidase forms. 2. The low-molecular-weight forms of acid 8-galactosidase undergo salt-dependent aggregation. 3. The high-molecular-weight component...

molar yields up to 36% were reported by protecting the product in situ against the hydrolytic activity of the same enzyme.'O} However, due to its biological source, this enzyrne seems to be of Iimited availability. Recently we have described a new fi-galactosidase from B. cireulans showing an extremely high specificity for the sequence of Gal-fi(1 .3)-GalNAc-ev-OR.") Because al1 figalactosidase...

Arabidopsis ATSIP2 has recently been suggested to be a raffinose synthase gene. However, it has high amino acid identity to functionally characterized alkaline α-galactosidases from Cucumis melo and Zea mays. Using the Sf9 insect cell expression system, we demonstrate that recombinant ATSIP2 is a genuine alkaline α-galactosidase with a distinct substrate specificity for raffinose, and not a raf...