Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/99390
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°C, and LIG-III was found to be the most stable in the temperature range tested. The observed kD values at 28, 35, and 50°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 kD values were obtained. The pH stability showed the same trends. © 1992.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/0141-0229(92)90010-L
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0026864072&partnerID=40&md5=6bb1c0e70bbc521e00b493173078ee83
Date Issue: 1992
Appears in Collections:Unicamp - Artigos e Outros Documentos

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