Effective prevention of chill-haze in beer using an acid proline-specific endoprotease from Aspergillus niger.
Chill-haze formation during beer production is known to involve polyphenols that interact with proline-rich proteins. We hypothesized that incubating beer wort with a proline-specific protease would extensively hydrolyze these proline-rich proteins, yielding a peptide fraction that is unable to form a haze. Predigestion of the proline-rich wheat gliadin with different proteases pointed toward a strong haze-suppressing effect by a proline-specific enzyme. This finding was confirmed in small-scale brewing experiments using a recently identified proline-specific protease with an acidic pH optimum. Subsequent pilot plant trials demonstrated that, upon its addition during the fermentation phase of beer brewing, even low levels of this acidic enzyme effectively prevented chill-haze formation in bottled beer. Results of beer foam stability measurements indicated that the enzyme treatment leaves the beer foam almost unaffected. In combination with the enzyme's cost-effectiveness and regulatory status, these preliminary test results seem to favor further industrial development of this enzymatic beer stabilization method.
Lopez
Michel
M
DSM Food Specialties, Post Office Box 1, 2600 MA Delft, The Netherlands.
Edens
Luppo
L
D001234:Aspergillus niger / Q000201:enzymology; D001515:Beer / Q000032:analysis*; D002392:Catechin / Q000378:metabolism; D005419:Flavonoids / Q000032:analysis; D005511:Food Handling / Q000379:methods*; D005524:Food Technology / Q000379:methods; D005903:Gliadin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010636:Phenols / Q000032:analysis; D010940:Plant Proteins / Q000378:metabolism; D059808:Polyphenols; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*
D005419:Flavonoids; D010636:Phenols; D010940:Plant Proteins; D059808:Polyphenols; D002392:Catechin; D005903:Gliadin; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases