Enzyme isolated from a Bifidobacterium
AssigneeArla Foods Amba
InventorsFlemming Jørgensen, Ole Cai Hansen, Peter Stougaard
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Abstract
The present invention concerns a new β-galactosidase with transgalactosylating activity isolated from Bifidobacterium bifidum and a truncated enzyme where the C-terminal end of the β-galactosidase protein has been deleted, resulting in an enzyme with a higher transgalactosylating activity than hydrolase activity. When lactose is used as a substrate, galacto-oligosaccharides are products of the transgalactosylase activity. Galacto-oligosaccharides enhance growth of health-promoting Bifidobacterium that may be used in a number of applications in the dairy industry.
Claims12
An isolated or purified enzyme comprising residues 1-1174 of SEQ ID NO:2, or a fragment thereof having transgalactosylating activity, wherein, the ratio of transgalactosylating activity to β-galactosidase activity in a solution of 100 g/L lactose at 37° C. that is higher than 1:1.
An isolated or purified enzyme comprising residues 1-1604 of SEQ ID NO:2, or a fragment thereof having transgalactosylating activity, wherein the ratio of transgalactosylating activity to β-galactosidase activity in a solution of 100 g/L lactose at 37° C. that is higher than 1:1.
An isolated or purified enzyme comprising residues 1-1327 of SEQ ID NO:2, or a fragment thereof having transgalactosylating activity, wherein the ratio of transgalactosylating activity to β-galactosidase activity in a solution of 100 g/L lactose at 37° C. that is higher than 1:1.
An isolated or purified enzyme comprising residues 1-983 of SEQ ID NO:2, or a fragment thereof having transgalactosylating activity, wherein the ratio of transgalactosylating activity to β-galactosidase activity in a solution of 100 g/L lactose at 37° C. that is higher than 1:1.
An isolated or purified fragment of SEQ ID NO:2 having a transgalactosylating activity, wherein said fragment has the amino acid sequence of SEQ ID NO:2 truncated at C-terminal and wherein the ratio of transgalactosylating activity to β-galactosidase activity in a solution of 100 g/L lactose at 37° C. is higher than 1:1.
Dependencies are inferred from the claim text.