%0 Journal Article
%T Purification and characterization of a thermostable alkaline protease produced by Yarrowia lipolytica
%A Hern¨¢ndez-Mart¨ªnez
%A R.
%A Sancho-Solano
%A A.
%A Loera-Corral
%A O.
%A Rojo-Dom¨ªnguez
%A A.
%A Regalado-Gonz¨¢lez
%A C.
%A Huerta-Ochoa
%A S.
%A Prado-Barrag¨¢n
%A L.A.
%J Revista mexicana de ingenier¨ªa qu¨ªmica
%D 2011
%I Universidad Aut¨®noma Metropolitana Unidad Iztapalapa
%X purification of the extracellular prote ase produced by yarrowia lipolytica was realized in fo ur steps: ammonium sulfate precipitation, anionic exchange (2x) and gel filtration. the enzyme showed m olecular weight of 61.5 kda (sds-page) and optimum activity at 52.4¡ãc at ph 10-11. the thermal stability was modified in presence of ca2+ (10 mm) providing an in crease of 73, 6 and 11% at 40, 50 and 60¡ãc respectively. the thermodynamic parameters (enthalpy and entropy) indicate that the stability of the enzyme is not provided by non-covalent linkages. furthermore the ion ca2+ is important for thermodynamic stabilization of the enzymatic structure. the proteolytic activity was inhibited by pmsf; suggesting that the enzyme can be classify in the serine protease family. the results of thermodynamic stability allow classifying the protease studied as thermostable. the importance of the ca2+ on the thermostability was corroborated; this is the first report on thermal stability and thermodynamic properties of proteases produced by y. lipolytica.
%K yarrowia lipolytica
%K protease
%K thermostable
%K thermodynamic stability.
%U http://www.scielo.org.mx/scielo.php?script=sci_abstract&pid=S1665-27382011000200017&lng=en&nrm=iso&tlng=en