Patent classifications
A23L2/66
EFFECTIVE PLANT PROTEIN DRINK STABILIZERS COMPRISING COLLOIDAL MICROCRYSTALLINE CELLULOSE MADE FROM NON-DISSOLVING CELLULOSE PULP
Provided is a co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps that is useful for stabilizing plant protein based drinks. Also provided are plant protein drink compositions stabilized using the co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps. Also provided are methods of stabilizing plant protein drink compositions using the co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps.
EFFECTIVE PLANT PROTEIN DRINK STABILIZERS COMPRISING COLLOIDAL MICROCRYSTALLINE CELLULOSE MADE FROM NON-DISSOLVING CELLULOSE PULP
Provided is a co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps that is useful for stabilizing plant protein based drinks. Also provided are plant protein drink compositions stabilized using the co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps. Also provided are methods of stabilizing plant protein drink compositions using the co-attrited MCC/CMC stabilizer composition containing MCC made from non-dissolving cellulose pulps.
Beverage product with free divalent cations protein aggregation and a method producing thereof
The invention relates to a method of producing a shelf stable ready-to-drink beverage product, comprising the steps of: providing an ingredient composition comprising micellar caseins and whey protein, having a total protein concentration of 1.5-8 wt. %, and wherein the composition has a casein to whey protein ratio of 90/10-60/40, adding divalent cations to provide a concentration of 3-20 mM free divalent cations in the ingredient composition, and 0.025-0.3 wt % of a stabilizing system comprising hydrocolloids, and subsequently heat treating the ingredient composition at ultra high temperature (UHT) at 135-150° C. for 3-30 s to form agglomerated proteins comprising casein and beta-lactoglobulin from the whey protein, the agglomerates having a size of 5-30 microns mean diameter D(4,3) as measured by laser diffraction. The invention also relates to a shelf stable ready-to-drink beverage product comprising aggregated proteins comprising micellar caseins and whey protein aggregates, wherein the product has a pH of 6.6-7.2, 1.5-8.0 wt. % milk proteins, a casein to whey protein ratio of 90/10-60/40, and a concentration of 3-20 mM divalent cations, and the aggregates are of 5-30 microns mean diameter D(4,3) as measured by laser diffraction.
Beverage product with free divalent cations protein aggregation and a method producing thereof
The invention relates to a method of producing a shelf stable ready-to-drink beverage product, comprising the steps of: providing an ingredient composition comprising micellar caseins and whey protein, having a total protein concentration of 1.5-8 wt. %, and wherein the composition has a casein to whey protein ratio of 90/10-60/40, adding divalent cations to provide a concentration of 3-20 mM free divalent cations in the ingredient composition, and 0.025-0.3 wt % of a stabilizing system comprising hydrocolloids, and subsequently heat treating the ingredient composition at ultra high temperature (UHT) at 135-150° C. for 3-30 s to form agglomerated proteins comprising casein and beta-lactoglobulin from the whey protein, the agglomerates having a size of 5-30 microns mean diameter D(4,3) as measured by laser diffraction. The invention also relates to a shelf stable ready-to-drink beverage product comprising aggregated proteins comprising micellar caseins and whey protein aggregates, wherein the product has a pH of 6.6-7.2, 1.5-8.0 wt. % milk proteins, a casein to whey protein ratio of 90/10-60/40, and a concentration of 3-20 mM divalent cations, and the aggregates are of 5-30 microns mean diameter D(4,3) as measured by laser diffraction.
FIBROIN-DERIVED PROTEIN COMPOSITION
A protein composition derived from silk fibroin, which composition possesses enhanced solubility and stability in aqueous solutions. The primary amino acid sequence of native fibroin is modified in the SDP such that cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains are reduced or eliminated. Additionally, the composition can have a serine content that is reduced by greater than 40% compared to native fibroin protein, and the average molecular weight of the SDP is less than about 100 kDa.
FIBROIN-DERIVED PROTEIN COMPOSITION
A protein composition derived from silk fibroin, which composition possesses enhanced solubility and stability in aqueous solutions. The primary amino acid sequence of native fibroin is modified in the SDP such that cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains are reduced or eliminated. Additionally, the composition can have a serine content that is reduced by greater than 40% compared to native fibroin protein, and the average molecular weight of the SDP is less than about 100 kDa.
FOOD OR BEVERAGE PRODUCT WITH AGGLOMERATED PEA PROTEIN
The present invention relates to a method of producing a food or beverage product, in particular to a method for forming agglomerated pea proteins in an ingredient composition. The invention also relates food or beverage product comprising agglomerated pea proteins.
FOOD OR BEVERAGE PRODUCT WITH AGGLOMERATED PEA PROTEIN
The present invention relates to a method of producing a food or beverage product, in particular to a method for forming agglomerated pea proteins in an ingredient composition. The invention also relates food or beverage product comprising agglomerated pea proteins.
A SUNFLOWER SEED PROTEIN ISOLATE AND A PROCESS FOR PRODUCING THE SAME
A process for preparing a sunflower seed protein isolate and a protein isolate which is obtainable by such process. The process comprises the following steps: mixing a defatted seed meal with an aqueous NaCl solution at a basic pH; separating said solubilised protein solution from solids; diafiltering said solubilised protein solution through an ultrafiltration membrane system using an aqueous NaCl diafiltration NaCl solution and at least 2 diavolumes of said aqueous NaCl diafiltration solution, diafiltering said NaCl-diafiltered protein; concentrating said purified protein solution; and drying said purified protein concentrate to obtain a protein isolate.
Polypeptide for use in the protection of oxygen sensitive gram-positive bacteria
The invention concerns a Reg3α polypeptide (also known as Hepatocarcinoma-Intestine-Pancreas/Pancreatitis Associated Protein (HIP/PAP)) for use in the protection of oxygen sensitive gram-positive bacteria, compositions comprising the polypeptide and their use. The inventors have shown that an increase in the concentration of the h Reg3α lectin into the gastrointestinal tract (GIT) lumen of hReg3α-transgenic mice induced significant changes in the composition of the gut microbiota, and dramatically improved host resistance to intestinal inflammation. hReg3α exerted a potent antioxidant activity on intestinal epithelial cells during colitis, and in particular the ROS scavenging activity, in particular, by promoting the survival of highly oxygen sensitive bacteria. Inventors also showed that h Reg3α-transgenic mice resist better to DSS-induced colitis after antibiotherapy. Thus, the invention concerns a Reg3α polypeptide for use in the protection of oxygen sensitive gram-positive bacteria, notably the Ruminococcaceae, such as Faecalibacterium prausnitzii, and/or the Lachnospiraceae, such as Roseburia intestinalis; pharmaceutical compositions comprising the polypeptide and their use; and the use of this polypeptide for promoting ex vivo growth of oxygen sensitive gram-positive bacteria. The Reg3α polypeptide may be used for preventing or treating microbiota-related disease and/or disorder, particularly selected from inflammatory bowel disease (IBD), colitis, gastrointestinal infections, irritable bowel syndrome and other gastrointestinal functional diseases, gastrointestinal tract cancer, metabolic syndrome and obesity, diabetes, liver diseases, allergic diseases, neurodegenerative diseases and psychological disorders.