National Research Council of Canada

Ozymes

Stephan Grosse

Peter C K Lau

Kofi Abokitse

Hélène Bergeron

Zhizhuang Xiao

Helene Bergeron

Peter Ck Lau

An isolated chimeric recombinant protein has cutinase activity. The protein includes a cutinase catalytic domain and a polymer binding domain operably linked by a proline/threonine-rich linker domain. The proline/threonine-rich linker domain includes at least 50% proline or threonine residues over a stretch of 15 to 55 consecutive amino acids.

Multi-domain enzymes having cutinase activity, compositions comprising same and uses thereof

Multi-domain recombinant proteins have a cutinase catalytic domain. The cutinase catalytic domain is a modular domain, which may be combined with other protein domains that also function in a modular fashion. For example, the cutinase catalytic domain can be operably linked to a polymer binding domain via a linker domain (e.g., a threonine/proline-rich linker polypeptide). The cutinase catalytic domain can be from an endogenous cutinase having a multi-domain modular organization, such as from the actinobacterium. The recombinant proteins are used in compositions, methods and uses, such as for use in industrial applications.

Using site-directed mutagenesis to mutate thepectate lyase gene, variants ofpectate lyase with improved thermostability and/or enzymatic activity have been expressed in, and then isolated and purified. The mutantpectate lyases are more effective than the wild-type enzyme, also expressed in, in removing pectic compounds from natural hemp fiber.

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Longueuil, Canada

Stephan Grosse