Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1119240
Research center of Embrapa/Collection: Embrapa Gado de Corte - Artigo em periódico indexado (ALICE)
Date Issued: 2019
Type of Material: Artigo em periódico indexado (ALICE)
Authors: 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.
Additional Information: 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.
Title: Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
Publisher: Biocatalysis and Agricultural Biotechnology, v. 21, 2019.
Language: en
Keywords: Endo-xylanase
Purification Aspergillus sp
Fruit juice clarification
Description: 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 μmol/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 β-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.
Data Created: 2020-01-23
Appears in Collections:Artigo em periódico indexado (CNPGC)

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