Novel GH10 Xylanase, with a Fibronectin Type 3 Domain, from
            <i>Cellulosimicrobium</i>
            sp. Strain HY-13, a Bacterium in the Gut of
            <i>Eisenia fetida</i>

Kim, Do Young; Han, Mi Kyung; Park, Doo Sang; Lee, Jong Suk; Oh, Hyun Woo; Shin, Dong‐Ha; Jeong, Tae Sook; Kim, Sung Uk; Bae, Kyung Sook; Son, Kwang Hee; Park, Ho Yong

doi:10.1128/aem.01075-09

Cited by 44 publications

(58 citation statements)

References 19 publications

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“…Therefore, increasing attention has been focused on exploring lignocellulase genes from diverse organisms, including free-living bacteria and fungi (45) as well as gut microbiomes of lignocellulose-consuming ruminants and insects (14,18,24,46). Termites feature differentiated body plans, including masticating organs, enlarged hindguts, symbiotic systems, and enriched digestive enzymes, for thriving on complex diets consisting of different plant components in different termite species (2).…”

mentioning

confidence: 99%

Microbiome of Fungus-Growing Termites: a New Reservoir for Lignocellulase Genes

Liu

Yan

Zhang

et al. 2011

Appl Environ Microbiol

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Fungus-growing termites play an important role in lignocellulose degradation and carbon mineralization in tropical and subtropical regions, but the degradation potentiality of their gut microbiota has long been neglected. The high quality and quantity of intestinal microbial DNA are indispensable for exploring new cellulose genes from termites by function-based screening. Here, using a refined intestinal microbial DNA extraction method followed by multiple-displacement amplification (MDA), a fosmid library was constructed from the total microbial DNA isolated from the gut of a termite growing in fungi. Functional screening for endoglucanase, cellobiohydrolase, ␤-glucosidase, and xylanase resulted in 12 ␤-glucosidase-positive clones and one xylanase-positive clone. The sequencing result of the xylanase-positive clone revealed an 1,818-bp open reading frame (ORF) encoding a 64.5-kDa multidomain endo-1,4-␤-xylanase, designated Xyl6E7, which consisted of an N-terminal GH11 family catalytic domain, a CBM_4_9 domain, and a Listeria-Bacteroides repeat domain. Xyl6E7 was a highly active, substrate-specific, and endo-acting alkaline xylanase with considerably wide pH tolerance and stability but extremely low thermostability.

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confidence: 99%

Microbiome of Fungus-Growing Termites: a New Reservoir for Lignocellulase Genes

Liu

Yan

Zhang

et al. 2011

Appl Environ Microbiol

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“…The greatest redox activity was found at a rate of 800 mg and higher doses affected survival of E. foetida. It is possible that some of the chromium redox reactions occur in the gastrointestinal tract where there is significant secretion of calcium carbonate (Laverack, 1963) and significant populations of bacteria with enzymatic activity (Kim et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

The influence of potassium dichromate on growth and survival of the vermicomposting earthworm Eisenia foetida

Tabche¹,

Cabriales²,

Maldonado-Vega³

et al. 2017

Afr. J. Biotechnol.

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-1 substrate) applied to a vermicomposting system which was inoculated with 30 earthworms per chamber. Earthworm growth, estimated by weight, showed a quadratic response (p = 0.03) with the lowest estimated growth at a dose of 435 mg K 2 Cr 2 O 7 kg -1 . Chromium (Cr) concentration increments were positively associated to mortality in adults and cocoons (p < 0.01), and total Cr accumulation in earthworms (p < 0.01). The accumulation of chromium in worms, is an indicator of the capacity of worms to resist different doses of potassium dichromate and, the effect on accumulation of Cr (VI) in vermicomposting was higher (p = 0.11). The difference of potassium dichromate in worms could indicate the oxide reduction in E. fetidae.

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“…Little is known about the function(s) of FNIII domains in amylases. Published reports about FNIII domains in carbohydrate-acting enzymes do not show a clear common function, with results pointing at possible roles in substrate binding or enzymatic activity (38)(39)(40)(41)(42)(43). So far, there are no reports of FNIII domains in prokaryotes with a function in protein-protein interactions.…”

Section: Discussionmentioning

confidence: 96%

Degradation of Granular Starch by the Bacterium Microbacterium aurum Strain B8.A Involves a Modular α-Amylase Enzyme System with FNIII and CBM25 Domains

Valk

Eeuwema

Sarian

et al. 2015

Appl Environ Microbiol

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The bacterium Microbacterium aurum strain B8.A, originally isolated from a potato plant wastewater facility, is able to degrade different types of starch granules. Here we report the characterization of an unusually large, multidomain M. aurum B8.A ␣-amylase enzyme (MaAmyA). MaAmyA is a 1,417-amino-acid (aa) protein with a predicted molecular mass of 148 kDa. Sequence analysis of MaAmyA showed that its catalytic core is a family GH13_32 ␣-amylase with the typical ABC domain structure, followed by a fibronectin (FNIII) domain, two carbohydrate binding modules (CBM25), and another three FNIII domains. Recombinant expression and purification yielded an enzyme with the ability to degrade wheat and potato starch granules by introducing pores. Characterization of various truncated mutants of MaAmyA revealed a direct relationship between the presence of CBM25 domains and the ability of MaAmyA to form pores in starch granules, while the FNIII domains most likely function as stable linkers. At the C terminus, MaAmyA carries a 300-aa domain which is uniquely associated with large multidomain amylases; its function remains to be elucidated. We concluded that M. aurum B8.A employs a multidomain enzyme system to initiate degradation of starch granules via pore formation. Starch is an excellent carbon and energy source for many microorganisms, which employ a dedicated set of proteins for extracellular hydrolysis of this polysaccharide, uptake of shorter oligosaccharides into the cell, and further degradation into glucose. Most studies on degradation of starch by microbial enzymes have focused on soluble starch. This has resulted in the identification and characterization of a large variety of enzymes cleaving either ␣(1¡4) or ␣(1¡6) linkages in amylose and amylopectin. Most of these enzymes belong to the glycoside hydrolase 13 (GH13) family (1). Sequence diversity is such that, at the moment, the GH13 family contains a total of 40 subfamilies (1). Most of the new members in subfamilies are identified in DNA sequencing projects, and biochemical information about the activity and specificity of these potentially new enzymes is highly lagging.Many plants produce starch in a granular form for the storage of carbohydrates. The crystallinity of such granules varies with the plant source. Potato starch granules have a relatively high degree of crystallinity, making them notoriously resistant to bacterial and fungal degradation (2-4). Nevertheless, some microorganisms have been reported to employ enzymes that are able to digest granular starch (5, 6).Amylases found to be involved in granular starch degradation are often multidomain enzymes that include one or more carbohydrate binding modules (CBMs), which aid in the binding of the enzyme to the granular substrate (7-10).In previous work, various bacteria able to grow on potato starch granules as a carbon source were isolated, and their enzymatic degradation mechanism was evaluated. Initially, this resulted in the identification of an enzyme mechanism involving peeling off layer afte...

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Novel GH10 Xylanase, with a Fibronectin Type 3 Domain, from Cellulosimicrobium sp. Strain HY-13, a Bacterium in the Gut of Eisenia fetida

Cited by 44 publications

References 19 publications

Microbiome of Fungus-Growing Termites: a New Reservoir for Lignocellulase Genes

Microbiome of Fungus-Growing Termites: a New Reservoir for Lignocellulase Genes

The influence of potassium dichromate on growth and survival of the vermicomposting earthworm Eisenia foetida

Degradation of Granular Starch by the Bacterium Microbacterium aurum Strain B8.A Involves a Modular α-Amylase Enzyme System with FNIII and CBM25 Domains

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