Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/329024
Type: Artigo
Title: Biochemical Characterization, Thermal Stability, And Partial Sequence Of A Novel Exo-polygalacturonase From The Thermophilic Fungus Rhizomucor Pusillus A13.36 Obtained By Submerged Cultivation
Author: Trindade
Lucas Vinicius; Desagiacomo
Carla; Teixeira de Moraes Polizeli
Maria de Lourdes; de Lima Damasio
Andre Ricardo; Furuyama Lima
Aline Margarete; Gomes
Eleni; Bonilla-Rodriguez
Gustavo Orlando
Abstract: This work reports the production of an exo-polygalacturonase (exo-PG) by Rhizomucor pusillus A13.36 in submerged cultivation (SmC) in a shaker at 45 degrees C for 96 h. A single pectinase was found and purified in order to analyze its thermal stability, by salt precipitation and hydrophobic interaction chromatography. The pectinase has an estimated Mw of approximately 43.5-47 kDa and optimum pH of 4.0 but is stable in pH ranging from 3.5 to 9.5 and has an optimum temperature of 61 degrees C. It presents thermal stability between 30 and 60 degrees C, has 70% activation in the presence of Ca2+, and was tested using citrus pectin with a degree of methyl esterification (DE) of 26% E-a(d) for irreversible denaturation was 125.5 kJ/mol with positive variations of entropy and enthalpy for that and Delta G((d)) values were around 50 kJ/mol. The hydrolysis of polygalacturonate was analyzed by capillary electrophoresis which displayed a pattern of sequential hydrolysis (exo). The partial identification of the primary sequence was done by MS MALDI-TOF and a comparison with data banks showed the highest identity of the sequenced fragments of exo-PG from R. pusillus with an exo-pectinase from Aspergillus fumigatus. Pectin hydrolysis showed a sigmoidal curve for the Michaelis-Menten plot.
Subject: Fusarium-solani
Protein
Thermostability
Pectinase
Enzymes
Endoglucanase
Cooperativity
Fermentation
Perspectives
Binding
Editor: Hindawi Publishing Corp
New York
Citation: Biomed Research International. Hindawi Publishing Corp, p. , 2016.
Rights: aberto
Identifier DOI: 10.1155/2016/8653583
Address: https://www.hindawi.com/journals/bmri/2016/8653583/
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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