The invention relates to method for the efficient expression and purification and application of a recombinant fusion protein of MANNase and homologues thereof and GLP-1. Through genetic recombination technology, soluble proteins are obtained by using high density fermentation of Pichia pastoris to induce secretory expression, followed by isolation and purification by filtration and concentration to obtain high yield of target proteins. The high fermentation expression and simple isolation steps solve the limitations of the current GLP-1 analogs such as low drug yield, high cost and the need for frequent injections. More importantly, the fusion protein has hypoglycemic effect not only by injection, but also by oral administration for hypoglycemia and weight reduction, which has good application value in obese and pre-diabetic patients. It also provides a basis for further research on the mechanism of hypoglycemia and weight loss of mannanase and homologues thereof with GLP-1 recombinant fusion protein.

A novel isolated Pichia stipitis strain is provided. The strain is capable of fermenting at least a pentose sugar in the presence of one or more inhibitory substances to produce ethanol. A method of utilizing the strain to produce ethanol is also provided.

The present disclosure provides compositions and methods related to the production of human milk oligosaccharides (HMOs). In particular, the present disclosure provides compositions and methods for converting lactose and N-acetylglucosamine (GlcNAc) into N-acetyllactosamine (LacNAc)-enriched galactooligosaccharide (GOS) compositions using novel β-hexosyl-transferase (BHT) enzymes.

A novel method of growing fungi is disclosed which uses an engineered artificial media and produces high density filamentous fungi biomats that can be harvested with a minimum of processing and from which fungal products such as antibiotics, proteins, and lipids can be isolated, the method resulting in lowered fungus cultivation costs for energy usage, oxygenation, water usage and waste stream production.

Provided is a method for preparing Rebaudioside J using an enzymatic method, comprising using rebaudioside A as a substrate, and making the substrate, in the presence of a glycosyl donor, react under the catalysis of a UDP-glycosyltransferase-containing recombinant cell and/or UDP-glycosyltransferase prepared therefrom to generate Rebaudioside J.

A process for the preparation of bio-based malonic acid and crystalline calcium malonate is provided. The calcium malonate is highly pure and provides a source of malonic acid made from a renewable carbon source rather than existing processes which rely on the use of petroleum-based products. The calcium malonate provides an improved source of malonic acid, which is important to many industrial processes.

Methods and materials related to producing D-lactic acid are disclosed. Specifically, isolated synthetic or natural nucleic acids, synthetic or natural polypeptides, host cells, and methods and materials for producing D-lactic acid by direct fermentation from carbon sources are disclosed, along with methods of preparing D-lactic acid polymers.

The invention relates to a recombinant yeast wherein the PEP4 gene is inactivated. Said yeast is useful for the production of oligopeptides.

A novel isolated Pichia stipitis strain is provided. The strain is capable of fermenting at least a pentose sugar in the presence of one or more inhibitory substances to produce ethanol. A method of utilizing the strain to produce ethanol is also provided.

The biological production of beta-hydroxyisovalerate (βHIV) using at least one non-natural enzyme. The non-natural enzyme for the biologically-derived βHIV provides more beta-hydroxyisovalerate synthase activity than the wild-type parent. The non-natural enzyme having one or more modifications of substrate-specificity positions. The non-natural enzyme can be expressed in a microorganism, such as a yeast or bacteria, wherein the microorganism comprises an active βHIV metabolic pathway for the production of βHIV. Alternatively, the non-natural enzyme can be a βHIV synthase used to produce βHIV in a cell-free environment. The biological derivation of βHIV eliminates toxic by-products and impurities that result from the chemical production of βHIV, such that βHIV produced by a non-natural enzyme prior to any isolation or purification process has not been in substantial contact with any halogen-containing component.