• Main Author: Charles Gerday
• Other Authors: The Pennsylvania State University CiteSeerX Archives
• Format: Text
• Language: English
• Subjects: Antarctic; The Antarctic; Antarc*
• Online Access: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.1030.5708; http://orbi.ulg.ac.be/bitstream/2268/15969/1/JBC_2002_xyl.pdf

Xylanases are generally classified into glycosyl hydro-lase families 10 and 11 and are found to frequently have an inverse relationship between their pI and molecular mass values. However, we have isolated a psychrophilic xylanase that belongs to family 8 and which has both a high pI and high molecular mass. This novel xylanase, isolated from the Antarctic bacterium Pseudoalteromo-nas haloplanktis, is not homologous to family 10 or 11 enzymes but has 20–30 % identity with family 8 members. NMR analysis shows that this enzyme hydrolyzes with inversion of anomeric configuration, in contrast to other known xylanases which are retaining. No cellu-lase, chitosanase or lichenase activity was detected. It appears to be functionally similar to family 11 xyla-nases. It hydrolyzes xylan to principally xylotriose and