Production Dynamics and Characterization of Chitinolytic System of Streptomyces sp. NK1057, a Well Equipped Chitin Degrader

Streptomyces sp. NK 1057 produced four extracellular chitinases. Two (62 and 48 kDa) were endochitinaseswhile the other two (35 and 28 kDa) had chitobiosidaseactivity. Chi62 was produced in early growth phase whereas the other three were produced later. Chi48 was optimally active at pH 4.0 and 60 °C whereas Chi35 was optimally active at pH 6.0 and 40 °C. Both the enzymes had fairly good pH and temperature stability up to 50 °C, with Chi48 being more thermostable than Chi35. Chi48 was significantly inhibited by N-acetylglucosaminebut not by Hg²⁺ and the reverse was true for Chi35. Chi48 and Chi35 had isoelectric points of 5.1 and 6.0 and the N-terminal amino acid sequence of Chi35 determined uptofour amino acids, was Gln–Ser–Pro– Gly. Chi62 and Chi48 were able to inhibit the germination of Fusariumoxysporum spores by 57.4 and 61.2% respectively whereas; Chi35 and Chi28 did so by only 14.1 and 3.8%, suggesting endochitinaseto possess antifungal activity. Only Chi28 exhibited a lytic activity, 0.022 U ml^–1, towards Micrococcus lysodeikticus cells.