The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%. The disclosure realizes efficient expression and high purification of porcine myoglobin from various steps such as synthesis, fermentation and purification of porcine myoglobin, and provides broad prospects for industrial production of porcine myoglobin.

The invention relates to cleaning compositions comprising a fructan degrading enzyme and at least one cleaning component, and use of such compositions for cleaning of an item such as a textile or a surface.

The technology described herein is directed to combinations and combinations for reducing the symptoms of digestive conditions, e.g., caused by ingestion of FODMAPs.

The present invention relates to an oral care composition comprising a fructanase, use of said composition as medicaments, use of said composition in treatment of oral disease, methods of treatment comprising administering said composition to a human or animal subject, methods of removing biofilm comprising contacting the biofilm with said composition, kits of parts comprising said composition, and fructanases.

A modified endoinulinase is provided, comprising modified wild-type T. purpuregenus endoinulinase, or a functional fragment thereof, in which an amino acid residue at each one of one or more positions corresponding to 128, 316, 344, 350 or 504 of wild-type T. purpuregenus endoinulinase is substituted, wherein: (i) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; and a threonine residue corresponding to T504 is substituted with M, S or Y; and optionally an alanine residue corresponding to A316 is substituted with T, S, C or M; (ii) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; a threonine residue corresponding to T504 is substituted with M, S or Y; and a glutamine residue corresponding to Q350 is substituted with L, G, A, V or I; or (iii) a tyrosine residue corresponding to Y128 is substituted with H, K or R.

A stable fructooligosaccharide (FOS) composition is produced from a raw material containing sucrose by enzymatic activity in aqueous mixture, chromatographically separating non-FOS carbohydrates from the aqueous mixture and evaporating the aqueous mixture to yield a syrupy FOS composition of at least 65 °Bx, wherein at least part or essentially all of the organic acids and ions is formed in situ.

The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%. The disclosure realizes efficient expression and high purification of porcine myoglobin from various steps such as synthesis, fermentation and purification of porcine myoglobin, and provides broad prospects for industrial production of porcine myoglobin.

The present invention relates to a method for reducing fructan in a fructan-containing food product, comprising adding an invertase belonging to enzyme classification EC 3.2.1.26 to the food product, and incubating the food product with the invertase, wherein fructan in the fructan-containing food product is hydrolysed. The invention further relates to the use of an invertase belonging to enzyme classification EC. 3.2.1.26 for the preparation of a medicament or a dietary supplement for the treatment of a person suffering from irritable bowel syndrome. Invertase (EC 3.2.1.26) may optionally by further combined with inulinase (EC3.2.1.7) and/or beta-fructosidase (EC 3.2.1.80).

A modified endoinulinase is provided, comprising modified wild-type T. purpuregenus endoinulinase, or a functional fragment thereof, in which an amino acid residue at each one of one or more positions corresponding to 128, 316, 344, 350 or 504 of wild-type T. purpuregenus endoinulinase is substituted, wherein: (i) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; and a threonine residue corresponding to T504 is substituted with M, S or Y; and optionally an alanine residue corresponding to A316 is substituted with T, S, C or M; (ii) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; a threonine residue corresponding to T504 is substituted with M, S or Y; and a glutamine residue corresponding to Q350 is substituted with L, G, A, V or I; or (iii) a tyrosine residue corresponding to Y128 is substituted with H, K or R.

A modified endoinulinase is provided, comprising modified wild-type T. purpuregenus endoinulinase, or a functional fragment thereof, in which an amino acid residue at each one of one or more positions corresponding to 128, 316, 344, 350 or 504 of wild-type T. purpuregenus endoinulinase is substituted, wherein: (i) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; and a threonine residue corresponding to T504 is substituted with M, S or Y; and optionally an alanine residue corresponding to A316 is substituted with T, S, C or M; (ii) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; a threonine residue corresponding to T504 is substituted with M, S or Y; and a glutamine residue corresponding to Q350 is substituted with L, G, A, V or I; or (iii) a tyrosine residue corresponding to Y128 is substituted with H, K or R.