Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,<i>Vibrio</i>sp. Strain MA-138

Tanaka, Megumi; Umemoto, Yoshiaki; Okamura, Hirokazu; Nakano, Daiichirou; Tamaru, Yutaka; Araki, Toshimitsu

doi:10.1271/bbb.80521

Cited by 27 publications

(13 citation statements)

References 59 publications

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“…CBM6 is often coupled to a GH16 catalytic domain [26], which has been described as acting against substrates that posses β-1,3 linkages such as lichenan, laminarin and curdlan. CBM27 is a protein domain that binds to mannose polymers, and is usually tied to GH26, β-mannosidase or β-xylosidase, forming a multidomain protein [20,27]. …”

Section: Resultsmentioning

confidence: 99%

Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi

Cairo

Leonardo

Alvarez

et al. 2011

Biotechnol Biofuels

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BackgroundLignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and the production of bioproducts derived from plant cell wall biomass are complex and lengthy processes. The understanding of termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.ResultsThe study herein shows comprehensive functional characterization of crude body extracts from Coptotermes gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases and accessory proteins responsible for plant biomass conversion. The crude protein extract from C. gestroi was enzymatically efficient over a broad pH range on a series of natural polysaccharides, formed by glucose-, xylose-, mannan- and/or arabinose-containing polymers, linked by various types of glycosidic bonds, as well as ramification types. Our proteomic approach successfully identified a large number of relevant polypeptides in the C. gestroi digestome. A total of 55 different proteins were identified and classified into 29 CAZy families. Based on the total number of peptides identified, the majority of components found in the C. gestroi digestome were cellulose-degrading enzymes. Xylanolytic enzymes, mannan- hydrolytic enzymes, pectinases and starch-degrading and debranching enzymes were also identified. Our strategy enabled validation of liquid chromatography with tandem mass spectrometry recognized proteins, by enzymatic functional assays and by following the degradation products of specific 8-amino-1,3,6-pyrenetrisulfonic acid labeled oligosaccharides through capillary zone electrophoresis.ConclusionsHere we describe the first global study on the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced their ability to cleave all types of glycosidic bonds present in plant polysaccharides. The comprehensive proteomic analysis, revealed a complete collection of hydrolytic enzymes including cellulases (GH1, GH3, GH5, GH7, GH9 and CBM 6), hemicellulases (GH2, GH10, GH11, GH16, GH43 and CBM 27) and pectinases (GH28 and GH29).

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Section: Resultsmentioning

confidence: 99%

Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi

Cairo

Leonardo

Alvarez

et al. 2011

Biotechnol Biofuels

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“…Several bacterial β-mannanase genes have been cloned and characterized, including those from Bacillus circulans, 11) Vibrio sp. strain MA-138 12) B. circulans K-1, 13) and Saccharophagus degradans. 14) The enzyme is used in the preparation of mannooligosaccharides in the pharmaceutical and energy industries.…”

Section: )mentioning

confidence: 99%

“…β-Mannanases been characterized in both mesophilic and psychrophilic bacteria, such as Pseudoalteromonas issachenkonii, 15) Vibrio sp. strain MA-138 12) and Flavobacterium sp. 16) Further, β-mannanases have also been isolated from fungi, such as Aspergillus niger, 17) as well as plants species, such as ripe tomato fruit.…”

Section: )mentioning

confidence: 99%

Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity

Hakamada

Ohkubo²,

Ohashi

2014

Bioscience, Biotechnology, and Biochemistry

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Marine bacterium Reinekea sp. KIT-YO10 was isolated from the seashore of Kanazawa Port in Japan as a seaweed-degrading bacterium. Homology between KIT-YO10 16S rDNA and the 16S rDNA of Reinekea blandensis and Reinekea marinisedimentorum was 96.4 and 95.4%, respectively. Endo-1,4-β-D-mannanase (β-mannanase, EC 3.2.1.78) from Reinekea sp. KIT-YO10 was purified 29.4-fold to a 21% yield using anion exchange chromatography. The purified enzyme had a molecular mass of 44.3 kDa, as estimated by SDS-PAGE. Furthermore, the purified enzyme displayed high specificity for konjac glucomannan, with no secondary agarase and arginase activity detected. Hydrolysis of konjac glucomannan and locust bean gum yielded oligosaccharides, compatible with an endo mode of substrate depolymerization. The purified enzyme possessed transglycosylation activity when mannooligosaccharides (mannotriose or mannotetraose) were used as substrates. Optimal pH and temperature were determined to be 8.0 and 70 °C, respectively. It showed thermostability at temperatures from 20 to 50 °C and alkaline stability up to pH 10.0. The current enzyme was thermostable and thermophile compared to the β-mannanase of other marine bacteria.

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“…Indeed, deletion of the CBM27 domain from TpMan had no affect on enzyme specificity (Table 2). In contrast, Man5C from Vibrio sp., a GH5 mannanase with a CBM27 accessory domain, showed strong positive interaction of the accessory domain with enzyme kinetics improving catalytic efficiency (k cat /K m ) (Tanaka et al, 2009). On the other hand, Man5C was isolated from a mesophilic bacterium and shares only 37% of amino acid sequence identity with TpMan thus suggesting distinctive roles for the accessory domain.…”

Section: How Useful Is the Cbm27 Accessory Domain For Catalytic Functmentioning

confidence: 99%

“…Both enzymes are nonthermophilic proteins and are poorly related to bacterial b-mannanases because of their low sequence similarity and high degree of glycosylation. Several b-mannanases from both eukaryotic and prokaryotic organisms display high affinity for glucomannans (Pressey, 1989;Tenkanen et al, 1997;Hilge et al, 1998;Tailford et al, 2009;Tanaka et al, 2009); however, the identification of glucose binding sites and their respective mode of interaction remain unknown.…”

Section: Introductionmentioning

confidence: 99%

Molecular insights into substrate specificity and thermal stability of a bacterial GH5-CBM27 endo-1,4-β-d-mannanase

Santos

Paiva

Meza

et al. 2012

Journal of Structural Biology

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The breakdown of β-1,4-mannoside linkages in a variety of mannan-containing polysaccharides is of great importance in industrial processes such as kraft pulp delignification, food processing and production of second-generation biofuels, which puts a premium on studies regarding the prospection and engineering of β-mannanases. In this work, a two-domain β-mannanase from Thermotoga petrophila that encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, was functionally and structurally characterized. Kinetic and thermal denaturation experiments showed that the CBM27 domain provided thermo-protection to the catalytic domain, while no contribution on enzymatic activity was observed. The structure of the catalytic domain determined by SIRAS revealed a canonical (α/β)(8)-barrel scaffold surrounded by loops and short helices that form the catalytic interface. Several structurally related ligand molecules interacting with TpMan were solved at high-resolution and resulted in a wide-range representation of the subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 directly involved in glucose binding.

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Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,Vibriosp. Strain MA-138

Cited by 27 publications

References 59 publications

Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi

Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi

Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity

Molecular insights into substrate specificity and thermal stability of a bacterial GH5-CBM27 endo-1,4-β-d-mannanase

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