Distinct actions by Paenibacillus sp. strain E18 α-L-arabinofuranosidases and xylanase in xylan degradation.

ABSTRACT: We cloned a Paenibacillus sp. strain E18 5.3-kb xylanolytic gene cluster that contains three open reading frames encoding two family 43 α-L-arabinofuranosidases (Abf43A and Abf43B) and one family 10 xylanase (XynBE18). The deduced amino acid sequences of Abf43A and Abf43B were at most 68% and 63% identical to those of two putative family 43 proteins from Clostridium sp. strain DL-VIII (EHI98634.1 and EHI98635.1), respectively, but were only 11% identical to each other. Recombinant Abf43A and Abf43B had similar activities at 45°C and pH 6.0 but varied in thermostabilities and substrate specificities. Abf43B was active against only 4-nitrophenyl α-L-arabinofuranoside, whereas Abf43A acted on 4-nitrophenyl α-L-arabinofuranoside, wheat arabinoxylan, 4-nitrophenyl α-D-xylopyranoside, and sugar

SUBMITTER: Shi P 

PROVIDER: S-EPMC3592258 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature