Abstract: A multivalent antigen binding protein comprises a single polypeptide chain comprising, in series, two or more single domain binding units which are preferably heavy chain variable domains derived from an immunoglobulin naturally devoid of light chains. Methods for their production and uses thereof, in particular for diagnosis, immunoassay and purification methods are disclosed.

Abstract: A multivalent antigen binding protein comprises a single polypeptide chain comprising, in series, two or more single domain binding units which are preferably heavy chain variable domains derived from an immunoglobulin naturally devoid of light chains. Methods for their production and uses thereof, in particular for diagnosis, immunoassay and purification methods are disclosed.

Abstract: The production of an active Pseudomonas glumae lipase isolated from P. glumae PG1 (CBS 322.89) and other lipases suitable for application in detergent systems is described in homologous, but particularly in heterologous hosts, e.g. Bacillus subtilis. For the latter a "helper function" or "lipase-specific stabilization/translocation protein" is needed, for which a gene is provided which, when expressed in concert with the lipase gene, can improve the stabilization of the intermediates involved in the production and translocation/secretion of the lipase. The hosts are transformed by recombinant DNA methods and modified lipases can be made by site-directed mutation or classical mutation techniques. The lipase gene and the gene encoding the helper function can be part of one operon that can be transcribed to form a polycistronic messenger or be present as separate genes yielding two mRNA's on transcription. The production level can be further improved by optimising the regulation sequences.

Abstract: Lipase enzymes including mutant lipase enzymes, e.g. from Pseudomonas species, are produced and modified by recombinant DNA technique. The enzymes are applicable in detergent and cleaning compositions, with advantages for example of improved stability to proteolytic digestion.

Abstract: The production of an active Pseudomonas glumae lipase isolated from P. glumae PG1 (CBS 322.89) and other lipases suitable for application in detergent systems is described in homologous, but particularly in heterologous hosts, e.g. Bacillus subtilis. For the latter a "helper function" or "lipase-specific stabilization/translocation protein" is needed, for which a gene is provided which, when expressed in concert with the lipase gene, can improve the stabilization of the intermediates involved in the production and translocation/secretion of the lipase. The hosts are transformed by recombinant DNA methods and modified lipases can be made by site-directed mutation or classical mutation techniques. The lipase gene and the gene encoding the helper function can be part of one operon that can be transcribed to form a polycistronic messenger or be present as separate genes yielding two mRNA's on transcription. The production level can be further improved by optimizing the regulation sequences.