Biochemical Characterization of Low Molecular Weight Thermostable Xylanase from Aspergillus fumigatus JCM 10253

2021 ◽  
Vol 57 (S1) ◽  
pp. S98-S106
Author(s):  
S. Paramjeet ◽  
P. Manasa ◽  
N. Korrapati
Keyword(s):  
Molecular Weight ◽  
Aspergillus Fumigatus ◽  
Biochemical Characterization ◽  
Low Molecular Weight ◽  
Thermostable Xylanase

scholarly journals Purification and characterization of a low molecular weight xylanase from solid-state cultures of Aspergillus fumigatus Fresenius

1999 ◽  
Vol 30 (2) ◽  
pp. 114-119 ◽  
Author(s):  
Claudio Henrique Cerri e Silva ◽  
Jurgen Puls ◽  
Marcelo Valle de Sousa ◽  
Edivaldo Ximenes Ferreira Filho
Keyword(s):  
Molecular Weight ◽  
Solid State ◽  
Aspergillus Fumigatus ◽  
Gel Filtration ◽  
Low Molecular Weight ◽  
Transferase Activity ◽  
Purification And Characterization ◽  
Apparent Homogeneity ◽  
Sds Page

A xylan-degrading enzyme (xylanase II) was purified to apparent homogeneity from solid-state cultures of Aspergillus fumigatus Fresenius. The molecular weight of xylanase II was found to be 19 and 8.5 kDa, as estimated by SDS-PAGE and gel filtration on FPLC, respectively. The purified enzyme was most active at 55 °C and pH 5.5. It was specific to xylan. The apparent Km and Vmax values on soluble and insoluble xylans from oat spelt and birchwood showed that xylanase II was most active on soluble birchwood xylan. Studies on hydrolysis products of various xylans and xylooligomers by xylanase II on HPLC showed that the enzyme released a range of products from xylobiose to xylohexaose, with a small amount of xylose from xylooligomers, and presented transferase activity.

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