The invention relates to the uses of a new characterized TET protein showed restricted to N-terminus glycine residues exopeptidase. The invention also relates to a method comprising said use of said new characterized TET protein as a N-terminus glycine residues specific exopeptidase. The invention further relates to a support wherein it is immobilized on said new characterized TET protein as a N-terminus glycine residues specific exopeptidase.

The invention relates to the uses of a new characterized TET protein showed restricted to N-terminus glycine residues exopeptidase. The invention also relates to a method comprising said use of said new characterized TET protein as a N-terminus glycine residues specific exopeptidase. The invention further relates to a support wherein it is immobilized on said new characterized TET protein as a N-terminus glycine residues specific exopeptidase.

The present invention is directed to a modified rapeseed protein isolate and to a process for making a modified rapeseed protein isolate with the aid of a peptidyl arginine deiminase.

The present invention is directed to a modified rapeseed protein isolate and to a process for making a modified rapeseed protein isolate with the aid of a peptidyl arginine deiminase.

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.

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.

A method of identifying a selected pollination window in a Poaceae crop by monitoring one or more environmental parameters and identifying a selected pollination window based upon the monitored parameters. The correct selection of parameters has been shown to markedly increase seed set, yield, and/or other desirable characteristics, including but not limited to preferred content of oil, starch, protein, and/or other nutritional components. Parameters may include one or more of: temperature, relative humidity, and vapor pressure deficit.

A method for unlocking bioactive proteins that can then be used to activate natural remedies. The method includes starting with Silica salt and water mixture. Then a base of whey protein concentrate is added to the mixture. The pH of the whey protein mixture is raised using a base. The pH is held at a level above 11 for at least two hours. After at least two hours an acid is then added to the mixture to bring the pH of the mixture below 3 pH. This will stop the activation process. After the unattached proteins are removed the protein mixture is then brought back to a normal pH level, around 4 pH.

Disclosed is a protein glutaminase having improved thermotolerance. A protein glutaminase comprising a polypeptide indicated in any among (1) to (3) has improved thermotolerance. (1) A polypeptide comprising a SEQ ID NO: 1 or 2 amino acid sequence; (2) a polypeptide wherein one or more amino acid residues are substituted, added, inserted or lost in the amino acid sequence indicated by SEQ ID NO: 1 or 2 and exhibiting the same thermotolerance as the amino acid sequence indicated by SEQ ID NO: 1 or 2: and (3) a polypeptide having at least 76% sequence identity with the amino acid sequence indicated by SEQ ID NO: 1 or 2 and having similar thermotolerance to a polypeptide comprising the amino acid sequence indicated by SEQ ID NO: 1 or 2.

Disclosed is a protein glutaminase having improved thermotolerance. A protein glutaminase comprising a polypeptide indicated in any among (1) to (3) has improved thermotolerance. (1) A polypeptide comprising a SEQ ID NO: 1 or 2 amino acid sequence; (2) a polypeptide wherein one or more amino acid residues are substituted, added, inserted or lost in the amino acid sequence indicated by SEQ ID NO: 1 or 2 and exhibiting the same thermotolerance as the amino acid sequence indicated by SEQ ID NO: 1 or 2: and (3) a polypeptide having at least 76% sequence identity with the amino acid sequence indicated by SEQ ID NO: 1 or 2 and having similar thermotolerance to a polypeptide comprising the amino acid sequence indicated by SEQ ID NO: 1 or 2.