Cellulosilyticum ruminicola, a newly described rumen bacterium that possesses redundant Fibrolytic-protein-encoding genes and degrades lignocellulose with multiple carbohydrateborne fibrolytic enzymes

Shichun Cai, Jiabao Li, Fen Ze Hu, Kegui Zhang, Yuanming Luo, Benjamin Janto, Robert J Boissy, Garth Ehrlich, Xiuzhu Dong

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Cellulosilyticum ruminicola 111 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola 111 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl esterases to break the interbridge cross-link, as well as the enzymes that degrade the glycosidic bonds. This bacterium appears to produce polymer hydrolases that act on both soluble and crystal celluloses. Approximately half of the cellulytic activities, including cellobiohydrolase (50%), feruloyl esterase (45%), and one third of xylanase (31%) and endoglucanase (36%) activities were bound to cellulosic fibers. However, only a minority of mannase (6.78%) and pectinase (1.76%) activities were fiber associated. Strain H1 seems to degrade the plant-derived polysaccharides by producing individual fibrolytic enzymes, whereas the majority of polysaccharide hydrolases contain carbohydrate-binding module. Cellulosome or cellulosomelike protein complex was never isolated from this bacterium. Thus, the fibrolytic enzyme production of strain H1 may represent a different strategy in cellulase organization used by most of other ruminal microbes, but it applies the fungal mode of cellulose production.

Original languageEnglish (US)
Pages (from-to)3818-3824
Number of pages7
JournalApplied and environmental microbiology
Volume76
Issue number12
DOIs
StatePublished - Jun 1 2010

Fingerprint

rumen bacteria
lignocellulose
Rumen
Cellulase
Cellulose 1,4-beta-Cellobiosidase
endo-1,4-beta-glucanase
cellulose 1,4-beta-cellobiosidase
enzyme
Bacteria
beta-mannosidase
yaks
bacterium
protein
gene
Hydrolases
xylanases
Enzymes
enzymes
hydrolases
polysaccharide

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

Cite this

Cellulosilyticum ruminicola, a newly described rumen bacterium that possesses redundant Fibrolytic-protein-encoding genes and degrades lignocellulose with multiple carbohydrateborne fibrolytic enzymes. / Cai, Shichun; Li, Jiabao; Ze Hu, Fen; Zhang, Kegui; Luo, Yuanming; Janto, Benjamin; Boissy, Robert J; Ehrlich, Garth; Dong, Xiuzhu.

In: Applied and environmental microbiology, Vol. 76, No. 12, 01.06.2010, p. 3818-3824.

Research output: Contribution to journalArticle

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abstract = "Cellulosilyticum ruminicola 111 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola 111 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl esterases to break the interbridge cross-link, as well as the enzymes that degrade the glycosidic bonds. This bacterium appears to produce polymer hydrolases that act on both soluble and crystal celluloses. Approximately half of the cellulytic activities, including cellobiohydrolase (50{\%}), feruloyl esterase (45{\%}), and one third of xylanase (31{\%}) and endoglucanase (36{\%}) activities were bound to cellulosic fibers. However, only a minority of mannase (6.78{\%}) and pectinase (1.76{\%}) activities were fiber associated. Strain H1 seems to degrade the plant-derived polysaccharides by producing individual fibrolytic enzymes, whereas the majority of polysaccharide hydrolases contain carbohydrate-binding module. Cellulosome or cellulosomelike protein complex was never isolated from this bacterium. Thus, the fibrolytic enzyme production of strain H1 may represent a different strategy in cellulase organization used by most of other ruminal microbes, but it applies the fungal mode of cellulose production.",
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AU - Li, Jiabao

AU - Ze Hu, Fen

AU - Zhang, Kegui

AU - Luo, Yuanming

AU - Janto, Benjamin

AU - Boissy, Robert J

AU - Ehrlich, Garth

AU - Dong, Xiuzhu

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N2 - Cellulosilyticum ruminicola 111 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola 111 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl esterases to break the interbridge cross-link, as well as the enzymes that degrade the glycosidic bonds. This bacterium appears to produce polymer hydrolases that act on both soluble and crystal celluloses. Approximately half of the cellulytic activities, including cellobiohydrolase (50%), feruloyl esterase (45%), and one third of xylanase (31%) and endoglucanase (36%) activities were bound to cellulosic fibers. However, only a minority of mannase (6.78%) and pectinase (1.76%) activities were fiber associated. Strain H1 seems to degrade the plant-derived polysaccharides by producing individual fibrolytic enzymes, whereas the majority of polysaccharide hydrolases contain carbohydrate-binding module. Cellulosome or cellulosomelike protein complex was never isolated from this bacterium. Thus, the fibrolytic enzyme production of strain H1 may represent a different strategy in cellulase organization used by most of other ruminal microbes, but it applies the fungal mode of cellulose production.

AB - Cellulosilyticum ruminicola 111 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola 111 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl esterases to break the interbridge cross-link, as well as the enzymes that degrade the glycosidic bonds. This bacterium appears to produce polymer hydrolases that act on both soluble and crystal celluloses. Approximately half of the cellulytic activities, including cellobiohydrolase (50%), feruloyl esterase (45%), and one third of xylanase (31%) and endoglucanase (36%) activities were bound to cellulosic fibers. However, only a minority of mannase (6.78%) and pectinase (1.76%) activities were fiber associated. Strain H1 seems to degrade the plant-derived polysaccharides by producing individual fibrolytic enzymes, whereas the majority of polysaccharide hydrolases contain carbohydrate-binding module. Cellulosome or cellulosomelike protein complex was never isolated from this bacterium. Thus, the fibrolytic enzyme production of strain H1 may represent a different strategy in cellulase organization used by most of other ruminal microbes, but it applies the fungal mode of cellulose production.

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