||Niu, Dandan; Tian, Xiaojing; Peace Mchunu, Nokuthula; Jia, Chao; Singh, Suren; Liu, Xiaoguang; Prior, Bernard A; Lu, Fuping.|
||Biochemical characterization of three Aspergillus niger ß-galactosidases|
||Electron. j. biotechnol;27:37-43, May. 2017. tab, ilus, graf.
||National Natural Science Foundation of China; . National Natural Science Foundation of Fujian Province, China; . Priming Scientific Research Foundation of Fuzhou University.
||Background: ß-Galactosidases catalyze both hydrolytic and transgalactosylation reactions and therefore have many applications in food, medical, and biotechnological fields. Aspergillus niger has been a main source of ß-galactosidase, but the properties of this enzyme are incompletely studied. Results: Three new ß-galactosidases belonging to glycosyl hydrolase family 35 from A. niger F0215 were cloned, expressed, and biochemically characterized. In addition to the known activity of LacA encoded by lacA, three putative ß-galactosidases, designated as LacB, LacC, and LacE encoded by the genes lacB, lacC, and lacE, respectively, were successfully cloned, sequenced, and expressed and secreted by Pichia pastoris. These three proteins and LacA have N-terminal signal sequences and are therefore predicted to be extracellular enzymes. They have the typical structure of fungal ß-galactosidases with defined hydrolytic and transgalactosylation activities on lactose. However, their activity properties differed. In particular, LacB and lacE displayed maximum hydrolytic activity at pH 45 and 50°C, while LacC exhibited maximum activity at pH 3.5 and 60°C. All ß-galactosidases performed transgalactosylation activity optimally in an acidic environment. Conclusions: Three new ß-galactosidases belonging to glycosyl hydrolase family 35 from A. niger F0215 were cloned and biochemically characterized. In addition to the known LacA, A. niger has at least three ß-galactosidase family members with remarkably different biochemical properties.|
||-Especificidade por Substrato|
Sequência de Aminoácidos
||CL1.1 - Biblioteca Central|