Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6

Fu, Wei; Han, Baoqin; Duan, Delin; Liu, Wanshun; Wang, Changhong

doi:10.1007/s10295-008-0365-2

Cited by 39 publications

(21 citation statements)

References 34 publications

(41 reference statements)

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“…The enzyme was stable under the conditions of this assay was determined by measuring the residual activity at pH 8.0 after 30 min incubation. With evident from (Aoki et al, 1990), that majority of agarases are optimally active in pH ranged between 6.5 and 7.5 and similar results were also observed (Fu et al, 2008). This effect had been studied for Alcaligenes sp.…”

Section: Enzyme Stability For Ph Profilessupporting

confidence: 53%

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Characterization and optimization of agarase from an estuarine Bacillus subtilis

Saraswathi¹,

Vasanthabharathi²,

Kalaiselvi³

et al. 2011

Afr. J. Microbiol. Res.

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A bacterium producing agarase was isolated from the vellar estuary and potential strain was identified as Bacillus subtilis. The ideal parameters was found to be of pH 8, temperature of 40°C and 3% of NaCl concentration for optimal growth and agarase activity. Agar as carbon source and yeast extract as nitrogen source was found to be suitable for optimum growth and agarase activity. The activity of enzyme obtained from the cell free filtrate was 15.2 U/L and the activity of the partially purified enzyme was 5.3 U/L and the purified enzyme activity was found to be 2.3 U/L. The stability of the partially purified enzyme on pH profile was found to be pH 8 and thermostability was found to be up to 40°C. The purified enzyme was determined to be homogeneous on the basis of SDS PAGE and had a molecular weight of 20 KDa.

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Section: Enzyme Stability For Ph Profilessupporting

confidence: 53%

“…where the enzyme was rapidly inactivated at temperatures above 30°C was also reported (Fu et al, 2008). The observed effect was contradicted (Lee et al, 2003) in Alcaligenes sp.…”

Section: Stability Of the Amylase Enzyme At Different Temperaturementioning

confidence: 54%

Characterization and optimization of agarase from an estuarine Bacillus subtilis

Saraswathi¹,

Vasanthabharathi²,

Kalaiselvi³

et al. 2011

Afr. J. Microbiol. Res.

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“…Enzymes in the β-agarolytic pathway β-Agarases, which selectively break β-(1,4) glycosidic linkages (G-β(1,4)-LA) through various mechanisms, have been reported in many taxonomically diverse microbial genera, including Cytophaga (van der Meulen and Harder 1976), Pseudomonas (Groleau and Yaphe 1977;Morrice et al 1983), Vibrio (Araki et al 1998;Dong et al 2007a;Fu et al 2008a;Liao et al 2011;Sugano et al 1993;Zhang and Sun 2007), Alteromonas (Kirimura et al 1999;Wang et al 2006a, b), Pseudoalteromonas (Lu et al 2009;Oh et al 2010), Flammeovirga (Yang et al 2011), and Agarivorans (Fu et al 2008b(Fu et al , 2009Lee et al 2006;Long et al 2010;Ohta et al 2005a). Based on the amino acid sequence similarity, β-agarases are found in four distinct GH families in the CAZy database: GH16, GH50, GH86, and GH118 (Michel et al 2006).…”

Section: Enzymology Of Agar Degradationmentioning

confidence: 99%

Agar degradation by microorganisms and agar-degrading enzymes

Chi

Chang

Hong

2012

Appl Microbiol Biotechnol

212

143

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Agar is a mixture of heterogeneous galactans, mainly composed of 3,6-anhydro-L-galactoses (or L-galactose-6-sulfates) D-galactoses and L-galactoses (routinely in the forms of 3,6-anhydro-L-galactoses or L-galactose-6-sulfates) alternately linked by β-(1,4) and α-(1,3) linkages. It is a major component of the cell walls of red algae and has been used in a variety of laboratory and industrial applications, owing to its jellifying properties. Many microorganisms that can hydrolyze and metabolize agar as a carbon and energy source have been identified in seawater and marine sediments. Agarolytic microorganisms commonly produce agarases, which catalyze the hydrolysis of agar. Numerous agarases have been identified in microorganisms of various genera. They are classified according to their cleavage pattern into three types-α-agarase, β-agarase, and β-porphyranase. Although, in a broad sense, many other agarases are involved in complete hydrolysis of agar, most of those identified are β-agarases. In this article we review agarolytic microorganisms and their agar-hydrolyzing systems, covering β-agarases as well as α-agarases, α-neoagarobiose hydrolases, and β-porphyranases, with emphasis on the recent discoveries. We also present an overview of the biochemical and structural characteristics of the various types of agarases. Further, we summarize and compare the agar-hydrolyzing systems of two specific microorganisms: Gram-negative Saccharophagus degradans 2-40 and Gram-positive Streptomyces coelicolor A3(2). We conclude with a brief discussion of the importance of agarases and their possible future application in producing oligosaccharides with various nutraceutical activities and in sustainably generating stock chemicals for biorefinement and bioenergy.

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“…SY37-12 29) S. degradans, 14) and Vibrio sp. F-6, 30) are typically obtained at 33-55°C. However, the enzyme used in this study had an optimum at 70°C.…”

Section: Substrate Specificitymentioning

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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Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6

Cited by 39 publications

References 34 publications

Characterization and optimization of agarase from an estuarine Bacillus subtilis

Characterization and optimization of agarase from an estuarine Bacillus subtilis

Agar degradation by microorganisms and agar-degrading enzymes

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

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