Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/81043
Type: Artigo de periódico
Title: LIGNIN PEROXIDASE FROM CHRYSONILIA-SITOPHILA - HEAT-DENATURATION KINETICS AND PH STABILITY
Author: FERRER, I
ESPOSITO, E
DURAN, N
Abstract: Many 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.
Editor: Butterworth-heinemann
Rights: fechado
Identifier DOI: 10.1016/0141-0229(92)90010-L
Date Issue: 1992
Appears in Collections:Unicamp - Artigos e Outros Documentos

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