Provided are compositions that include a metal-organic framework (MOF) including a framework defining an internal volume, an enzyme disposed within the internal volume, and a surfactant. Also provided are methods of making the compositions and their use.

Provided are compositions that include a metal-organic framework (MOF) including a framework defining an internal volume, an enzyme disposed within the internal volume, and a surfactant. Also provided are methods of making the compositions and their use.

The present invention relates to a composition or combination for the production of butanol and isopropanol, comprising an acetone-butanol-ethanol (ABE)-producing Clostridium strain and a genetically engineered B. subtilis strain, wherein said genetically engineered B. subtilis strain has been transformed by at least one polynucleotide molecule; the at least one polynucleotide molecule comprising a secondary alcohol dehydrogenase gene operably linked to at least one promoter. The invention also relates to methods of producing butanol and isopropanol in a co-culture, methods of producing butyrate, isopropanol and butanol in a co-culture and methods of producing esters.

The present invention relates to a composition or combination for the production of butanol and isopropanol, comprising an acetone-butanol-ethanol (ABE)-producing Clostridium strain and a genetically engineered B. subtilis strain, wherein said genetically engineered B. subtilis strain has been transformed by at least one polynucleotide molecule; the at least one polynucleotide molecule comprising a secondary alcohol dehydrogenase gene operably linked to at least one promoter. The invention also relates to methods of producing butanol and isopropanol in a co-culture, methods of producing butyrate, isopropanol and butanol in a co-culture and methods of producing esters.

Disclosed are compositions and methods relating to an improved hybrid lipase enzyme for reducing foaming in, for example, a carbohydrate fermentation process.

Disclosed are compositions and methods relating to an improved hybrid lipase enzyme for reducing foaming in, for example, a carbohydrate fermentation process.

Disclosed is a combination of two or more lipase enzymes, and its use for treating a lipid digestion deficiency and/or a digestive disorder. At least one lipase enzyme has a pH optimum at an acidic pH value, while at least one other lipase enzyme has a pH optimum at an alkalic pH value.

Disclosed is a combination of two or more lipase enzymes, and its use for treating a lipid digestion deficiency and/or a digestive disorder. At least one lipase enzyme has a pH optimum at an acidic pH value, while at least one other lipase enzyme has a pH optimum at an alkalic pH value.

A fusion protein is provided, comprising i) a biologically active polypeptide; and ii) a half-life extending polypeptide moiety comprising 2-80 units independently selected the amino acid sequences according to SEQ ID NO: 1: X1-X2-X3-X4-X5-X6-D-X8-X9-X10-X11 (SEQ ID NO: 1) in which, independently: X1 is P or absent; X2 is V or absent; X3 is P or T; X4 is P or T; X5 is T or V; X6 is D, G or T; X8 is A, Q or S; X9 is E, G or K; X10 is A, E P or T; and X11 is A, P or T. The half-life extending polypeptide moiety has a generally unfolded conformation and provides a fusion protein with a large hydrodynamic radius that may avoid renal clearance. As a result, the biological half-life of the fusion protein is increased and the biological effect of the biologically active polypeptide may thus be prolonged.

A fusion protein is provided, comprising i) a biologically active polypeptide; and ii) a half-life extending polypeptide moiety comprising 2-80 units independently selected the amino acid sequences according to SEQ ID NO: 1: X1-X2-X3-X4-X5-X6-D-X8-X9-X10-X11 (SEQ ID NO: 1) in which, independently: X1 is P or absent; X2 is V or absent; X3 is P or T; X4 is P or T; X5 is T or V; X6 is D, G or T; X8 is A, Q or S; X9 is E, G or K; X10 is A, E P or T; and X11 is A, P or T. The half-life extending polypeptide moiety has a generally unfolded conformation and provides a fusion protein with a large hydrodynamic radius that may avoid renal clearance. As a result, the biological half-life of the fusion protein is increased and the biological effect of the biologically active polypeptide may thus be prolonged.