Patent classifications
A23L27/21
Organic compounds
A stock solution comprising a compound of formula (I) ##STR00001## Wherein R.sub.1 together with the carbonyl group to which it is attached is a residue of a carboxylic acid, and NR.sub.2R.sub.3, in which R.sub.3 is H or together with R.sub.2 and the N-atom to which they are attached, a 5-membered ring, is a residue of an amino acid, in particular a proteinogenic amino acid, ornithine, gamma-aminobutyric acid or beta alanine, or a 1-amino cycloalkyl carboxylic acid.
Organic compounds
A stock solution comprising a compound of formula (I) ##STR00001## Wherein R.sub.1 together with the carbonyl group to which it is attached is a residue of a carboxylic acid, and NR.sub.2R.sub.3, in which R.sub.3 is H or together with R.sub.2 and the N-atom to which they are attached, a 5-membered ring, is a residue of an amino acid, in particular a proteinogenic amino acid, ornithine, gamma-aminobutyric acid or beta alanine, or a 1-amino cycloalkyl carboxylic acid.
DYNAMICALLY DELIVERING FAT AND FLAVOR POTENTIATORS TO FOODS AND METHODS OF USE THEREOF
A method and product comprising mixing at least one oil to a converted methylcellulose polymer to result in a methylcellulose polymer-oil mixture, mixing at least one hydrocolloid to the methylcellulose polymer-oil mixture and heating the methylcellulose polymer-oil mixture to result in a microgel structure; and entrapping at least one flavor potentiator within the microgel structure to result in a peptide-infused microgel structure.
DYNAMICALLY DELIVERING FAT AND FLAVOR POTENTIATORS TO FOODS AND METHODS OF USE THEREOF
A method and product comprising mixing at least one oil to a converted methylcellulose polymer to result in a methylcellulose polymer-oil mixture, mixing at least one hydrocolloid to the methylcellulose polymer-oil mixture and heating the methylcellulose polymer-oil mixture to result in a microgel structure; and entrapping at least one flavor potentiator within the microgel structure to result in a peptide-infused microgel structure.
FLAVOR COMPOSITION AND EDIBLE COMPOSITIONS CONTAINING SAME
A flavor composition containing at least one, two, three, four, five or more peptide compound(s) that can be used to enhance the taste of edible compositions including sweet goods, such as confectionery goods, and savory goods, such as pet foods.
FLAVOR COMPOSITION AND EDIBLE COMPOSITIONS CONTAINING SAME
A flavor composition containing at least one, two, three, four, five or more peptide compound(s) that can be used to enhance the taste of edible compositions including sweet goods, such as confectionery goods, and savory goods, such as pet foods.
N-acylated methionine derivatives as food flavoring compounds
A flavour composition comprising a compound of formula (I) ##STR00001## and edible salts thereof, wherein R.sub.1 is an alkyl residue containing 6 to 20 carbon atoms, or an alkene residue containing from 9 to 25 carbon atoms with 1 to 6 double bonds, R.sub.1 together with the carbonyl group to which it is attached is a residue of a carboxylic acid.
N-acylated methionine derivatives as food flavoring compounds
A flavour composition comprising a compound of formula (I) ##STR00001## and edible salts thereof, wherein R.sub.1 is an alkyl residue containing 6 to 20 carbon atoms, or an alkene residue containing from 9 to 25 carbon atoms with 1 to 6 double bonds, R.sub.1 together with the carbonyl group to which it is attached is a residue of a carboxylic acid.
Food Protein-Derived Peptides as Bitter Taste Blockers
Beef protein was hydrolyzed with each of six commercial enzymes (alcalase, chymotrypsin, trypsin, pepsin, flavourzyme, and thermoase). Electronic tongue measurements showed that the hydrolysates had significantly (p<0.05) lower bitter scores than quinine. Addition of the hydrolysates to quinine led to reduced bitterness intensity of quinine with trypsin and pepsin hydrolysates being the most effective. Addition of the hydrolysates to HEK293T cells that heterologously express one of the bitter taste receptors (T2R4) showed alcalase, thermoase, pepsin and trypsin hydrolysates as the most effective in reducing calcium mobilization. Eight peptides that were identified from the alcalase and chymotrypsin hydrolysates also suppressed bitter agonist-dependent calcium release from T2R4 and T2R14 with AGDDAPRAVF and ETSARHL being the most effective.
Food Protein-Derived Peptides as Bitter Taste Blockers
Beef protein was hydrolyzed with each of six commercial enzymes (alcalase, chymotrypsin, trypsin, pepsin, flavourzyme, and thermoase). Electronic tongue measurements showed that the hydrolysates had significantly (p<0.05) lower bitter scores than quinine. Addition of the hydrolysates to quinine led to reduced bitterness intensity of quinine with trypsin and pepsin hydrolysates being the most effective. Addition of the hydrolysates to HEK293T cells that heterologously express one of the bitter taste receptors (T2R4) showed alcalase, thermoase, pepsin and trypsin hydrolysates as the most effective in reducing calcium mobilization. Eight peptides that were identified from the alcalase and chymotrypsin hydrolysates also suppressed bitter agonist-dependent calcium release from T2R4 and T2R14 with AGDDAPRAVF and ETSARHL being the most effective.