Characterization of Novel Ribbed Mussel (Geukensia demissa) Enzymes for Lignin Deconstruction

A novel lignin-digesting enzyme has been identified within ribbed mussels (Geukensia demissa) protein extracts. Enzymatic activity is demonstrated through the use of several model lignin compounds (2,2′-azinobis-3-ethylbenzothiazoline-6-sulfonic acid, 2,6-dimethoxyphenol, veratryl alcohol, and guaiacol), as well as actual lignin isolated from biomasses (lignin alkali, softwood, oakwood, and hardwood). Also, a 3,5-dinitrosalicylic acid assay was used for the enzymatic activity of the extracted proteins from the mussel against lignin. For all assays, a positive relationship between the amount of crude mussel protein extract and lignin-modifying peroxidase activity was observed. Extracts from digestive tissues of ribbed mussels contained more lignin peroxidase activity than extracts from nondigestive tissue. This identified enzymatic activity may offer a new area of investigation in biofuel research. Cloning of the genes encoding lignocellulose-digesting enzymes and evaluation of pure mussel enzyme capabilities would appear promising.

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Publication Details

Journal
Journal of Shellfish Research
Published
2025-08-11
DOI
https://doi.org/10.2983/035.044.0207
Primary Topic
Enzyme-mediated dye degradation
Type
article
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article

Characterization of Novel Ribbed Mussel (Geukensia demissa) Enzymes for Lignin Deconstruction

David H. Kingsley, Matthew E. Smith, Aristides Marcano Olaizola, Ali Parsaeimehr et al.
Journal of Shellfish Research
Enzyme-mediated dye degradation
article

Characterization of Novel Ribbed Mussel (Geukensia demissa) Enzymes for Lignin Deconstruction

David H. Kingsley, Matthew E. Smith, Aristides Marcano Olaizola, Ali Parsaeimehr, Gulnihal Ozbay, Andrew F. Harron
article en

Abstract

A novel lignin-digesting enzyme has been identified within ribbed mussels (Geukensia demissa) protein extracts. Enzymatic activity is demonstrated through the use of several model lignin compounds (2,2′-azinobis-3-ethylbenzothiazoline-6-sulfonic acid, 2,6-dimethoxyphenol, veratryl alcohol, and guaiacol), as well as actual lignin isolated from biomasses (lignin alkali, softwood, oakwood, and hardwood). Also, a 3,5-dinitrosalicylic acid assay was used for the enzymatic activity of the extracted proteins from the mussel against lignin. For all assays, a positive relationship between the amount of crude mussel protein extract and lignin-modifying peroxidase activity was observed. Extracts from digestive tissues of ribbed mussels contained more lignin peroxidase activity than extracts from nondigestive tissue. This identified enzymatic activity may offer a new area of investigation in biofuel research. Cloning of the genes encoding lignocellulose-digesting enzymes and evaluation of pure mussel enzyme capabilities would appear promising.

Journal of Shellfish ResearchVol. 44(2)
Delaware State University (US), Agricultural Research Service (US), South Dakota State University (US), Department of Agriculture (PH)
Life below water
Openalex Percentile: Top 84%
Enzyme-mediated dye degradation
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