Lignocellulosic biomass degradation enzymes and characterization of cellulase and xylanase from Bosea sp. FBZP-16

Houfani, Aicha Asma; Anders, Nico; Loogen, Judith; Heyman, Benedikt; Azzouz, Zahra; Bettache, Azzeddine; Büchs, Jochen; Benallaoua, Saı̈d

doi:10.1007/s13399-021-02044-1

Cited by 2 publications

(1 citation statement)

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“…Among the hemicellulase enzymes, GH43 was the most abundant family in the present study. Previous studies have reported the enzyme activities of GH43 to be β-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8) and exo-β-1,3-galactanase (EC 3.2.1.145; ( Shrivastava, 2020 ), which are enzymes contributing to the degradation of xylan (the main component of hemicellulose) to xylose monomers ( Houfani et al, 2021 ). One major challenge in producing biofuels from lignocellulosic biomass by enzymatic hydrolysis is that hemicellulose and lignin create a protective barrier surrounding the cellulose.…”

Section: Discussionmentioning

confidence: 99%

Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics

et al. 2022

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Extremophiles provide a one-of-a-kind source of enzymes with properties that allow them to endure the rigorous industrial conversion of lignocellulose biomass into fermentable sugars. However, the fact that most of these organisms fail to grow under typical culture conditions limits the accessibility to these enzymes. In this study, we employed a functional metagenomics approach to identify carbohydrate-degrading enzymes from Ethiopian soda lakes, which are extreme environments harboring a high microbial diversity. Out of 21,000 clones screened for the five carbohydrate hydrolyzing enzymes, 408 clones were found positive. Cellulase and amylase, gave high hit ratio of 1:75 and 1:280, respectively. A total of 378 genes involved in the degradation of complex carbohydrates were identified by combining high-throughput sequencing of 22 selected clones and bioinformatics analysis using a customized workflow. Around 41% of the annotated genes belonged to the Glycoside Hydrolases (GH). Multiple GHs were identified, indicating the potential to discover novel CAZymes useful for the enzymatic degradation of lignocellulose biomass from the Ethiopian soda Lakes. More than 73% of the annotated GH genes were linked to bacterial origins, with Halomonas as the most likely source. Biochemical characterization of the three enzymes from the selected clones (amylase, cellulase, and pectinase) showed that they are active in elevated temperatures, high pH, and high salt concentrations. These properties strongly indicate that the evaluated enzymes have the potential to be used for applications in various industrial processes, particularly in biorefinery for lignocellulose biomass conversion.

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Section: Discussionmentioning

confidence: 99%