The present invention provides a system for recovering protein in a production process of an ultrahigh maltose syrup, including a saccharification tank, an enzyme preparation tank, a first plate heat exchanger, a second plate heat exchanger, a plate and frame filter, a buffer tank and a rotary drum filter. The present invention further provides a method of recovering protein by using the system. After the sugar liquid in the saccharification tank is stood, the protein floats at the upper part of the saccharification tank and the lower liquid is clear and transparent and thus the sugar liquid can be directly filtered. When the saccharification tank is discharged, the lower liquid is firstly discharged with the remaining liquid being bottoms containing protein. During a production process, enzymatic hydrolysis is performed for the sugar liquid containing protein before filtration to improve the filtration effect of the sugar liquid. Assisted by the plate and frame filter, protein can be recovered. The present invention improves the economic benefits, reduces the production costs, and thus solves the problem of difficulty in recovering protein in a production process of an ultrahigh maltose syrup.

Methods of forming an ingredient for human consumption are provided herein. The methods may include isolating one or more soluble polysaccharides from a biomass, generating one or more oligosaccharides from the biomass, and combining the one or more isolated soluble polysaccharides with the generated oligosaccharides to form the ingredient. Methods of pretreating a biomass are also provided. The methods may include administering a physical pretreatment to a biomass, administering a gentle pretreatment to the physically pretreated biomass, and administering a strong pretreatment to the gently pretreated biomass. Ingredients for human consumption are also provided.

Methods of forming an ingredient for human consumption are provided herein. The methods may include isolating one or more soluble polysaccharides from a biomass, generating one or more oligosaccharides from the biomass, and combining the one or more isolated soluble polysaccharides with the generated oligosaccharides to form the ingredient. Methods of pretreating a biomass are also provided. The methods may include administering a physical pretreatment to a biomass, administering a gentle pretreatment to the physically pretreated biomass, and administering a strong pretreatment to the gently pretreated biomass. Ingredients for human consumption are also provided.

This disclosure is in the technical field of synthetic biology and metabolic engineering. More particularly, this disclosure is in the technical field of cultivation or fermentation of metabolically engineered cells. This disclosure provides a method for the production of a mixture of at least two different oligosaccharides by a cell as well as the purification of at least one of the oligosaccharides from the cultivation. In addition, this disclosure provides a method for the production of a mixture of at least two different oligosaccharides by a metabolically engineered cell as well as the purification of at least one of the oligosaccharides from the cultivation.

The usefulness of β-galactosidases derived from Bacillus circulans is further enhanced. A modified β-galactosidase in which one or more amino acids selected from the group consisting of proline 182 (P182), tyrosine 187 (Y187), serine 188 (S188), tryptophan 405 (W405), alanine 406 (A406), glutamine 407 (Q407), tyrosine 449 (Y449), threonine 483 (T483), serine 512 (S512), serine 531 (S531), threonine 533 (T533), serine 534 (S534), asparagine 550 (N550), glutamine 551 (Q551), tryptophan 593 (W593), tyrosine 598 (Y598), proline 602 (P602), proline 604 (P604), tyrosine 609 (Y609), lysine 612 (K612), and tyrosine 615 (Y615), or an amino acid(s) corresponding thereto, has/have been substituted by other amino acid in a β-galactosidase consisting of the amino acid sequence of any of SEQ ID NOs. 1 to 4 or an amino acid sequence having 90% or more identity to the amino acid sequence set forth in any of SEQ ID NOs. 1 to 4.

The usefulness of β-galactosidases derived from Bacillus circulans is further enhanced. A modified β-galactosidase in which one or more amino acids selected from the group consisting of proline 182 (P182), tyrosine 187 (Y187), serine 188 (S188), tryptophan 405 (W405), alanine 406 (A406), glutamine 407 (Q407), tyrosine 449 (Y449), threonine 483 (T483), serine 512 (S512), serine 531 (S531), threonine 533 (T533), serine 534 (S534), asparagine 550 (N550), glutamine 551 (Q551), tryptophan 593 (W593), tyrosine 598 (Y598), proline 602 (P602), proline 604 (P604), tyrosine 609 (Y609), lysine 612 (K612), and tyrosine 615 (Y615), or an amino acid(s) corresponding thereto, has/have been substituted by other amino acid in a β-galactosidase consisting of the amino acid sequence of any of SEQ ID NOs. 1 to 4 or an amino acid sequence having 90% or more identity to the amino acid sequence set forth in any of SEQ ID NOs. 1 to 4.

The disclosure is in the technical field of synthetic biology and metabolic engineering. More particularly, the disclosure is in the technical field of cultivation or fermentation of metabolically engineered cells. The disclosure describes a cell metabolically engineered for production of an alpha-1,3 glycosylated form of fucose-alpha1,2-galactose-R (Fuc-a1,2-Gal-R). Furthermore, the disclosure provides a method for the production of an alpha-1,3 glycosylated form of Fuc-a1,2-Gal-R by a cell as well as the purification of the alpha-1,3 glycosylated form Fuc-a1,2-Gal-R from the cultivation.

The disclosure is in the technical field of synthetic biology and metabolic engineering. More particularly, the disclosure is in the technical field of cultivation or fermentation of metabolically engineered cells. The disclosure describes a cell metabolically engineered for production of an alpha-1,3 glycosylated form of fucose-alpha1,2-galactose-R (Fuc-a1,2-Gal-R). Furthermore, the disclosure provides a method for the production of an alpha-1,3 glycosylated form of Fuc-a1,2-Gal-R by a cell as well as the purification of the alpha-1,3 glycosylated form Fuc-a1,2-Gal-R from the cultivation.

Disclosed is a method for improving the productivity of 2′-fucosyllactose (2′-FL) through enzymatic treatment. Lactose used as a substrate in the stationary phase during culture is degraded by treatment with a small amount of enzyme, the resulting glucose is consumed to produce guanosine diphosphate-L-fucose as a precursor of 2′-fucosyllactose, and the use of lactose left after culture can be maximally utilized for the production of 2′-fucosyllactose. As a result, it is possible to increase the productivity of 2′-fucosyllactose in an economically efficient manner because additional glucose is not required while minimizing by-products.

A process to hydrolyze cellulose into cellobiose comprising the following steps: providing a reaction vessel; providing a Cellulomonas uda (ATCC 491) inoculum; exposing said Cellulomonas uda (ATCC 491) bacterium to a source of cellulose having a kappa number of less than 10 in an aqueous medium of pH of about 8 at a temperature ranging from 30° C. to 35° C. for a period of time ranging from 14 to 42 days; exposing the cellobiose to a bacterium or fungi or yeast, or combination which converts cellobiose to glucose or ethanol.