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Bioproduction of N-acetyl-glucosamine from colloidal α-chitin using an enzyme cocktail produced by Aeromonas caviae CHZ306.
Cardozo, Flávio Augusto; Facchinatto, William Marcondes; Colnago, Luiz Alberto; Campana-Filho, Sergio Paulo; Pessoa, Adalberto.
Afiliación
  • Cardozo FA; Department of Microbiology, Biomedical Sciences Institute, University of Sao Paulo, 1374 Professor Lineu Prestes Ave., São Paulo, SP, 05508-000, Brazil. flavio.acardozo@gmail.com.
  • Facchinatto WM; Sao Carlos Institute of Chemistry, University of Sao Paulo, Trabalhador Sao-Carlense Ave, 400, Sao Carlos, SP, 13560-970, Brazil.
  • Colnago LA; Embrapa Instrumentation, R. XV de Novembro, 1452, Sao Carlos, SP, 13560-970, Brazil.
  • Campana-Filho SP; Sao Carlos Institute of Chemistry, University of Sao Paulo, Trabalhador Sao-Carlense Ave, 400, Sao Carlos, SP, 13560-970, Brazil.
  • Pessoa A; Department of Biochemical and Pharmaceutical Technology, Faculty of Pharmaceutical Sciences, University of Sao Paulo, 580 Professor Lineu Prestes Ave, São Paulo, 05508-000, Brazil.
World J Microbiol Biotechnol ; 35(8): 114, 2019 Jul 22.
Article en En | MEDLINE | ID: mdl-31332537
N-acetyl-D-glucosamine (GlcNAc) is an important amino-monosaccharide with great potential for biotechnological applications. It has traditionally been produced by the chemical hydrolysis of chitin, despite certain industrial and environmental drawbacks, including acidic wastes, low yields and high costs. Therefore, enzymatic production has gained attention as a promising environmentally-friendly alternative to the chemical processes. In this study we demonstrate the GlcNAc bioproduction from colloidal α-chitin using an enzyme cocktail containing endochitinases and exochitinases (chitobiosidases and N-acetyl-glucosaminidases). The enzyme cocktail was extracted after fermentation in a bioreactor by Aeromonas caviae CHZ306, a chitinolytic marine bacterium with great potential for chitinase production. Hydrolysis parameters were studied in terms of temperature, pH, enzyme and substrate concentration, and reaction time, achieving over 90% GlcNAc yield within 6 h. The use of colloidal α-chitin as substrate showed a substantial improvement of GlcNAc yields, when compared with ß-chitin and α-chitin polymorphs. Such result is directly related to a significant decrease in crystallinity and viscosity from natural α-chitin, providing the chitinase with greater accessibility to the depolymerized chains. This study provides valuable information on the GlcNAc bioproduction from chitin using an enzymatic approach, addressing the key points for its production, including the enzyme cocktail composition and the substrate structures.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acetilglucosamina / Quitina / Aeromonas caviae Idioma: En Revista: World J Microbiol Biotechnol Año: 2019 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acetilglucosamina / Quitina / Aeromonas caviae Idioma: En Revista: World J Microbiol Biotechnol Año: 2019 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Alemania