%0 Journal Article %A Kolbe, Steffi %A Fischer, Sabine %A Becirevic, Ardina %A Hinz, Petra %A Schrempf, Hildgund %T The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene %D 1998 %J Microbiology, %V 144 %N 5 %P 1291-1297 %@ 1465-2080 %R https://doi.org/10.1099/00221287-144-5-1291 %K Streptomyces reticuli %K CHB2 %K α-chitin-binding protein %I Microbiology Society, %X When co-cultivated with chitin-containing fungi, Strepfomyces reticuli secretes the chitin-binding protein CHB2. Microscopical and immunological investigations revealed that CHBZ acts like a glue to mediate the contact between the fungal and the Streptomyces hyphae. CHBZ was purified to homogeneity, and the sequence of its N-terminal amino acids was determined and used to deduce an oligonucleotide, which was then used to probe a subgenomic library. The ch62 gene was cloned, sequenced and overexpressed. The deduced mature protein has a molecular mass of 18.6 kDa, and a large number of its amino acids are identical to those of CHBl from Streptomyces oliwaceowiridis. CHB2 effectively targets different types of α-chitin, but no other polysaccharide. The dissociation constant (Kd) for binding to purified crab shell chitin is 0 27 μM. Immunological studies suggest that homologues of CHBl and CHBZ are secreted by streptomycetes while growing in the presence of a-chitin-containing substrates. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-144-5-1291