Characterization of <i>Brettanomyces bruxellensis</i> Phenolic Acid Decarboxylase Enzyme Expressed in <i>Escherichia coli</i>

Brettanomyces yeasts are considered spoilage organisms in commercial fermentation settings; however, some historical beer styles and several modern specialty beer styles rely on Brettanomyces for unique aroma and flavor contributions. The organoleptic properties of beer utilizing intentional Brettanomyces fermentations can be unpredictable and inconsistent. This study investigates the contributions of Brettanomyces fermentations to volatile phenolic character by expression of phenolic acid decarboxylase enzyme cloned from B. bruxellensis. Protein was expressed and isolated from Escherichia cells. The enzyme has broad temperature and pH ranges, and showed variable activity against the most common potential hydroxycinnamic acid substrates.

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Publication Details

Journal
Journal of the American Society of Brewing Chemists
Published
2024-08-13
DOI
https://doi.org/10.1080/03610470.2024.2371744
Citations
2
Primary Topic
Biochemical and biochemical processes
Type
article
Field-Weighted Citation Impact
0.77
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article

Characterization of Brettanomyces bruxellensis Phenolic Acid Decarboxylase Enzyme Expressed in Escherichia coli

Michael Lentz
2 citations
Journal of the American Society of Brewing Chemists
Biochemical and biochemical processes
0.77
article

Characterization of Brettanomyces bruxellensis Phenolic Acid Decarboxylase Enzyme Expressed in Escherichia coli

Michael Lentz
article en
2 citations

Abstract

Brettanomyces yeasts are considered spoilage organisms in commercial fermentation settings; however, some historical beer styles and several modern specialty beer styles rely on Brettanomyces for unique aroma and flavor contributions. The organoleptic properties of beer utilizing intentional Brettanomyces fermentations can be unpredictable and inconsistent. This study investigates the contributions of Brettanomyces fermentations to volatile phenolic character by expression of phenolic acid decarboxylase enzyme cloned from B. bruxellensis. Protein was expressed and isolated from Escherichia cells. The enzyme has broad temperature and pH ranges, and showed variable activity against the most common potential hydroxycinnamic acid substrates.

Journal of the American Society of Brewing ChemistsVol. 82(4)
University of North Florida (US)
Zero hunger
Openalex Percentile: Top 28%
Biochemical and biochemical processes
0.77
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