Partial purification and characterisation of sugarcane neutral invertase.
Sugarcane neutral invertase (SNI) has been partially purified from mature sugarcane stem tissue to remove any potential competing activity. The enzyme is non-glycosylated and exhibits catalytic activity as a monomer, dimer and tetramer, most of the activity elutes as a monomer of native M(r) ca 60 k. The enzyme displays typical hyperbolic saturation kinetics for Suc hydrolysis. It has a K(m) of 9.8 mM for Suc and a pH optimum of 7.2. An Arrhenius plot shows the energy of activation of the enzyme for Suc to be 62.5 kJ mol-1 below 30 degrees and -11.6 kJ mol-1 above 30 degrees. SNI is inhibited by its products, with Fru being a more effective inhibitor than Glc. SNI is significantly inhibited by HgCl2, AgNO3, ZnCl2, CuSO4 and CoCl2 but not by CaCl2, MgCl2 or MnCl2. SNI showed no significant hydrolysis of cellobiose or trehalose.
Vorster
D J
DJ
Department of Biotechnology, South African Sugar Association Experiment Station, Mount Edgecombe, South Africa.
Botha
F C
FC
D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006031:Glycosylation; D006109:Poaceae / Q000201:enzymology*; D043324:beta-Fructofuranosidase
D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase