Abstract: 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.

Abstract: 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.

Abstract: 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 Kineococcus radiotolerans. The recombinant proteins are used in compositions, methods and uses, such as for use in industrial applications.

Abstract: 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 Kineococcus radiotolerans. The recombinant proteins are used in compositions, methods and uses, such as for use in industrial applications.

Abstract: The invention relates to a new “gene-switch” (cumate-inducible switch) for mammalian cells, having a mammalian promoter which has a TATA element and is linked to the coding sequence of CymR. This switch is as useful in the development of expression systems and cell-based assays for functional genomics as in the generation of viral vectors for gene therapy.

Abstract: Using site-directed mutagenesis to mutate the Xanthomonas campestris pectate lyase gene, variants of Xanthomonas campestris pectate lyase with improved thermostability and/or enzymatic activity have been expressed in Escherichia coli, and then isolated and purified. The mutant Xanthomonas campestris pectate lyases are more effective than the wild-type enzyme, also expressed in E. coli, in removing pectic compounds from natural hemp fiber.

Abstract: Using site-directed mutagenesis to mutate the Xanthomonas campestris pectate lyase gene, variants of Xanthomonas campestris pectate lyase with improved thermostability and/or enzymatic activity have been expressed in Escherichia coli, and then isolated and purified. The mutant Xanthomonas campestris pectate lyases are more effective than the wild-type enzyme, also expressed in E. coli, in removing pectic compounds from natural hemp fiber.

Abstract: The invention relates to a new “gene-switch” (cumate-inducible switch) for mammalian cells. This switch is as useful in the development of expression systems and cell-based assays for functional genomics as in the generation of viral vectors for gene therapy.

Abstract: The invention relates to a new “gene-switch” (cumate-inducible switch) for mammalian cells. This switch is as useful in the development of expression systems and cell-based assays for functional genomics as in the generation of viral vectors for gene therapy.

Abstract: Cyclopentanone 1,2-monooxygenase (CPMO) from Comamonas (previously Pseudomonas) sp. strain NCIMB 9872 carries out the second step of a degradation pathway that allows the bacterium to use cyclopentanol as a sole carbon source for growth. In the present invention there is reported the localization of the CPMO-encoding gene (cpnB) on a 4.3-kb SphI fragment, the determination of its sequence. The 550-amino acid CPMO polypeptide (Mr, 62,111) encoded by the gene was found to have 36.5% identity with the sequence of cyclohexanone 1,2-monooxygenase (CHMO) of Acinetobacter sp. strain NCIMB 9871. The 62-kDa CPMO was expressed in E. coli as an IPTG-inducible protein.

Abstract: The invention relates to a new strain of Pseudomonas putida (designated as HI-70) and to the isolation, cloning, and sequencing of a cyclododecanone monooxygenase-encoding gene (named cdnB) from said strain. The invention also relates to a new cyclododecanone monooxygenase and to a method of use of the cyclododecanone monooxygenase-encoding gene.

Abstract: 4-vinylguaiacol is produced using recombinant E. coli containing a decarboxylase gene from Bacillus pumilis in an aqueous fermentation broth and in an immobilized whole cell system. The 4-vinylguaiacol is extracted and recovered from an organic hydrocarbon solvent, preferably n-octane, whereby the product can readily be separated.

Abstract: The invention relates to a new strain of Pseudomonas putida (designated as HI-70) and to the isolation, cloning, and sequencing of a cyclododecanone monooxygenase-encoding gene (named cdnB) from said strain. The invention also relates to a new cyclododecanone monooxygenase and to a method of use of the cyclododecanone monooxygenase-encoding gene.

Abstract: Cyclopentanone 1,2-monooxygenase (CPMO) from Comamonas (previously Pseudomonas) sp. strain NCIMB 9872 carries out the second step of a degradation pathway that allows the bacterium to use cyclopentanol as a sole carbon source for growth. In the present invention there is reported the localization of the CPMO-encoding gene (cpnB) on a 4.3-kb SphI fragment, the determination of its sequence. The 550-amino acid CPMO polypeptide (Mt, 62,111) encoded by the gene was found to have 36.5% identity with the sequence of cyclohexanone 1,2-monooxygenase (CHMO) of Acinetobacter sp. strain NCIMB 9871. The 62-kDa CPMO was expressed in E. coli as an IPTG-inducible protein.

Abstract: The invention relates to a new “gene-switch” (cumate-inducible switch) for mammalian cells. This switch is as useful in the development of expression systems and cell-based assays for functional genomics as in the generation of viral vectors for gene therapy.