Digital Repository

A comparative study of chitin synthase activity in two Mortierella species

DSpace/Manakin Repository

Show simple item record Adjimani, Jonanthan P. en_US 2009-07-09T17:30:46Z 2009-07-09T17:30:46Z 1983-07-09T17:30:46Z
dc.description.abstract An in vitro investigation of some important factors controlling the activity of chitin synthase in cell-free extracts of two Mortierella species has been carried out. Mixed membrane fractions from mycelial homogenates of Mortierella candelabrum and Mortierella pusilla were found to catalyse the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine into an insoluble product characterized as chitin by its insolubility in weak acid and alkali, and the release of glucosamine and diacetylchitobiose on hydrolysis with a strong acid and chitinase, respectively. Apparent Km values for UDP-GlcNAc were 1.8 mM and 2.0 mM for M. pusilla and ~ candelabrum, respectively. Polyoxin D was found to be a very potent competitive inhibitor with values of the constant of inhibition, Ki' for both species about three orders of magnitude lower than theKm for UDP-GlcNAc. A divalent cation, Mg+2 , Mn+2 or Co+2 , was required for activity. N-acetylglucosamine, the monomer of chitin, stimulated the activity of the enzyme. The crude enzyme preparation of ~ candelabrum, unlike that of ~ pusilla, showed an absolute requirement for both Mg+2 and N-acetylglucosamine. Large differences in response to exogenous proteases were noted in the ratio of active to inactive chitin synthase of the two species. A fifteen fold or greater increase was obtained after treatment with acid protease (from Aspergillussaitoi) as compared to a two- to four-fold activation of the M. pusilla membrane preparation treated similarly. During storage at 4°C over 48 hours, an endogenous activation of chitin synthase of ~ pus ilIa was achieved, comparable to that obtained by exogenous protease treatment. The high speed supernatant of both species inhibited the chitin synthase activity of the mixed membrane fractions. The inhibitor of ~ pus ilIa was effective against the pre-activated enzyme whereas that of M. candelabrum inhibited the activated enzyme. Several possibilities are discussed as to the role of the different factors regulating the enzyme activity. The suggestion is made from the properties of chitin synthase in the two species that in vivo a delicate balance exists between the activation and inactivation of the enzyme which is responsible for the pattern of wall growth of each fungus. en_US
dc.language.iso eng en_US
dc.publisher Brock University en_US
dc.subject Mortierella. en_US
dc.subject Chitin. en_US
dc.title A comparative study of chitin synthase activity in two Mortierella species en_US
dc.type Electronic Thesis or Dissertation en_US M.Sc. Biological Sciences en_US Masters en_US
dc.contributor.department Department of Biological Sciences en_US Faculty of Mathematics and Science en_US

Files in this item

This item appears in the following Collection(s)

Show simple item record

Search The Repository


My Account


About the Digital Repository