LIGNIN PEROXIDASE FROM CHRYSONILIA-SITOPHILA - HEAT-DENATURATION KINETICS AND PH STABILITY

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dc.contributor.authorFERRER, I
dc.contributor.authorESPOSITO, E
dc.contributor.authorDURAN, N
dc.date.accessioned2025-01-23T19:22:09Z
dc.date.available2025-01-23T19:22:09Z
dc.date.issued1992
dc.description.abstractMany practical applications utilizing lignin peroxidases from Chrysonilia sitophila (TFB-27441 strain) have been proposed. However, more information regarding the stability of these enzymes was required to design and develop these technologies. Heat- and pH-denaturation studies were conducted on purified lignin peroxidase and on crude culture of lignin peroxidase from C. sitophila. The culture produced in a 15-l bioreactor with Fries medium was utilized to obtain purified lignin peroxidases. LIG-I, LIG-II, and LIG-III were tested in the range 28-50-degrees-C, and LIG-III was found to be the most stable in the temperature range tested. The observed k(D) values at 28, 35, and 50-degrees-C were 0.058, 0.095, and 0.111 h-1, respectively. Increasing the LIG-III concentration by 2.3-fold increased thermal stability by around twofold. The heat-denaturation kinetics under these conditions for all lignin peroxidases and for the crude culture were first-order. LIG-I and LIG-II appeared as the most representative enzymes in the crude culture, since similar k(D) values were obtained. The pH stability showed the same trends.
dc.fuente.origenWOS
dc.identifier.issn0141-0229
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/98975
dc.identifier.wosidWOS:A1992HN54400010
dc.issue.numero5
dc.language.isoen
dc.pagina.final406
dc.pagina.inicio402
dc.revistaEnzyme and microbial technology
dc.rightsacceso restringido
dc.subject.ods06 Clean Water and Sanitation
dc.subject.odspa06 Agua limpia y saneamiento
dc.titleLIGNIN PEROXIDASE FROM CHRYSONILIA-SITOPHILA - HEAT-DENATURATION KINETICS AND PH STABILITY
dc.typeartículo
dc.volumen14
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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