Data/hora: 19/06/2024 05:12:08

Biblioteca(s): 	Embrapa Gado de Corte.	
Data corrente: 	23/01/2020	
Data da última atualização: 	23/01/2020	
Autoria: 	SILVA, P. O. da; GUIMARÃES, N. C. de A.; SERPA, J. D. M.; MASUI, D. C.; MARCHETTI, C. R.; VERBISCK, N. V.; ZANOELO, F. F.; RULLER, R.; GIANNESI, G. C.	
Afiliação: 	Patricia Oliveira da Silva, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Nelciele Cavalieri de Alencar Guimarães, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; John Dayvan Maidana Serpa, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Douglas Chodi Masui, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Clarice Rossatto Marchetti, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; NEWTON VALERIO VERBISCK, CNPGC; Fabiana Fonseca Zanoelo, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Roberto Ruller, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Giovana Cristina Giannesi, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos.	
Título: 	Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.	
Ano de publicação: 	2019	
Fonte/Imprenta: 	Biocatalysis and Agricultural Biotechnology, v. 21, 2019.	
Idioma: 	Inglês	
Conteúdo: 	The endo-xylanase from Aspergillus japonicus (UFMS 48.136) was purified in a single step using carboximethylcellulose chromatographic column and applied in fruit juice clarification process and fruit peel waste hydrolysis. This purification procedure resulted in 38.9-fold purification of endo-xylanase with 83.3% final yield. MALDITOF analysis confirmed the molecular mass of 32 kDa. The optimal purified endo-xylanase activity was at a range of pH from 5.0 to 6.0 and from 50 to 60 +-C, retaining more than 70% of its activity at all pH studied (3.0?8.0) for 24 h at room temperature. The A. japonicus endo-xylanolytic activity stimulation curve was assayed in the presence of different birchwood xylan concentrations (ranging from 0.02 to 0.5% w/v) and the endoxylanase activity presented a Vmax of 467.4 +- 30.38 &#956;mol/min/mg, with a km of 2.59 +- 0.17 mg/mL, a kcat of 253.95 +- 16.51 s -1 and a kcat/km value of 98.05 +- 4.41 mL s -1 mg -1. The endo-xylanase was activated by Mn2þ (34.5%) and inhibited by Cu2þ (56.9%). The endo-xylanase was activated by &#946;-mercaptoethanol, Triton X-100, Tween-20, Tween-80 and ferulic acid. In the clarification assay, endo-xylanase successfully clarified the juices of mango (51.11%), banana (9.99%) and tangerine (8.54%). Furthermore, the enzyme also hydrolysed all fruit peel wastes that were tested. In summary, A. japonicus endo-xylanase showed potential for applications in fruit juice clarification and in the treatment of fruit peel wastes, and it is a good candidate for the food industry due to its wide pH stability under acidic conditions.	
Palavras-Chave: 	Endo-xylanase; Fruit juice clarification; Purification Aspergillus sp.	
Categoria do assunto: 	--	
URL: 	http://ainfo.cnptia.embrapa.br/digital/bitstream/item/209484/1/Application-of-an-endo-xylanase.pdf	
Registro original: 	Embrapa Gado de Corte (CNPGC)	
Exemplares: 	CNPGC - (17519-1) - UPC - AP - DD -  -  -  - DIS