1993FEMS Microbiology LettersOpen access

Arabinan degrading enzymes fromAspergillus nidulans: Induction and purification

Daniel Ramà n, P. van der Veen, Jaap Visser

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Abstract

The presence in Aspergillus nidulans of two enzymes related to the Aspergillus niger endo-arabinase and alpha-L-arabinofuranosidase B has been established using antibodies against the purified A. niger enzymes. Moreover, the absence of an equivalent in A. nidulans to the alpha-L-arabinofuranosidase A of A. niger has been confirmed both at the protein and at the DNA level. Both A. nidulans arabinases have been purified and physico-chemically and kinetically characterized. They have a much higher temperature optimum than the corresponding A. niger enzymes. The pattern of induction has been studied on media containing different carbon sources showing an important role of L-arabitol in the induction of these enzymes.

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The presence in Aspergillus nidulans of two enzymes related to the Aspergillus niger endo-arabinase and alpha-L-arabinofuranosidase B has been established using antibodies against the purified A. niger enzymes. Moreover, the absence of an equivalent in A. nidulans to the alpha-L-arabinofuranosidase A of A. niger has been confirmed both at the protein and at the DNA level. Both A. nidulans arabinases have been purified and physico-chemically and kinetically characterized. They have a much higher temperature optimum than the corresponding A. niger enzymes. The pattern of induction has been studied on media containing different carbon sources showing an important role of L-arabitol in the induction of these enzymes.

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Available abstract

The presence in Aspergillus nidulans of two enzymes related to the Aspergillus niger endo-arabinase and alpha-L-arabinofuranosidase B has been established using antibodies against the purified A. niger enzymes. Moreover, the absence of an equivalent in A. nidulans to the alpha-L-arabinofuranosidase A of A. niger has been confirmed both at the protein and at the DNA level. Both A. nidulans arabinases have been purified and physico-chemically and kinetically characterized. They have a much higher temperature optimum than the corresponding A. niger enzymes. The pattern of induction has been studied on media containing different carbon sources showing an important role of L-arabitol in the induction of these enzymes.

Key concepts: Aspergillus nidulans, Aspergillus niger, Enzyme, Biochemistry, Aspergillus, Chemistry, Biology, Microbiology

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