Behrends_1996_FEMS.Microbiol.Lett_143_191

Binding of (i) purified wild-type poly(3-hydroxybutyrate) (PHB) depolymerase PhaZ4 of Pseudomonas lemoignei, (ii) a purified truncated form of PhaZ4, which lacked 55 C-terminal amino acids and (iii) commercial lactate dehydrogenase to aqueous suspensions of PHB, chitin or cellulose was studied. Only the wild-type PHB depolymerase was specifically able to bind to PHB granules. No other combination of protein and polymeric substrate resulted in polymer-bound protein. Similar results were obtained for other PHB depolymerases. We concluded that the C-terminal amino acids of PHB depolymerases represent a PHB-specific binding domain or at least an essential part of it.