Characterization and partial purification of hypocrea jecorina qm9414 beta galactosidase.

Enzymes are protein molecules that catalyse a biochemical reaction and found in all living cells. They are usually obtained from plants, animals and microorganisms.ß-Galactosidase (ß-D-galactoside galactohydrolase, EC 3.2.1.23, the enzmye that hydrolyzes lactose into its component monosaccharide units of glucose and galactose.ß-Galactosidase can be used in solving the probleus associated with whey disposal lactose crystallization in frozen concentrated desserts and milk consumption by lactose-intolerant populations of the world. ß-Galactosidase deficiency is a wide spread problem occuring in approximately %70 of the world?s population. ß-Galactosidases are able to hydrolyse lactose without side reactions.Commercial ß-galactosidases have been purified in particular from Kluyveromyces lactis, Aspergillus niger or Escherichia coli. Its application to the hydrolysis of lactose in dairy products, such as milk and cheese whey, has received much attention in the last years. ß-Galactosidases are capable of catalyzing synthesis of certain oligosaccaharides via the galactosyl transfer reaction.The Hypocrea jecorina QM9414 is a fungus and industrially applied for the production of cellulolytic and hemicellulolytic enzymes.The objectives of this thesis are to determine the optimum conditions for ß-galactosidase induction and partial purification of the enzyme from H. jecorina.