Purification and characterisation of intracellular alpha-galactosidases from Acinetobacter sp.
Two alpha-galactosidases (Ag-I & Ag-II) were purified from Acinetobacter sp. Both the enzymes were monomeric with pH optima of 7.0 and molecular weight of 65 kDa for Ag-I and 37 kDa for Ag-II. The temperature optima for Ag-I was between 50 and 60 °C and that of Ag-II was 40 °C. Both the enzymes were strongly inhibited by metal ions Ag2+and Hg+, pCMB and SDS (1 %). The enzymes were found to be active on both natural and synthetic substrates. Artificial substrate, pNPGal, has shown more affinity to enzyme than natural substrate raffinose. The half-life (t1/2) of Ag-I varied from 1.85 h at 90 °C to 7.6 h at 70 °C.
Centre for Biotechnology, Institute of Science and Technology, Jawaharlal Nehru Technological University Hyderabad, Hyderabad, Telangana, India.
Sirisha
S
E
School of Agriculture, Food and Wine, The University of Adelaide, Waite Campus, Urbrae, SA, 5064, Australia.
Ravichandra
R
Potumarthi
Centre for Biotechnology, Institute of Science and Technology, Jawaharlal Nehru Technological University Hyderabad, Hyderabad, Telangana, India.
Naveen
N
A
Centre for Biotechnology, Institute of Science and Technology, Jawaharlal Nehru Technological University Hyderabad, Hyderabad, Telangana, India. mangamoori@gmail.com.
Lakshmi Narasu
LN
Mangamoori
Acinetobacter; Multiple forms; Purification; α-Galactosidases