Characterization of a novel β-agarase from an agar-degrading bacterium Catenovulum sp. X3

Xie, Wei; Lin, Bokun; Zhou, Zhengrong; Lu, Guoyong; Lun, Jingsheng; Xia, Changyan; Li, Shengkang; Huang, Zhong

doi:10.1007/s00253-012-4385-5

Cited by 61 publications

(39 citation statements)

References 23 publications

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“…Recently, another β-agarase gene, agaXa , was cloned from Catenovulum sp. X3, which is in the same genus as YM01 T [45]. AgaXa is also a thermostable agarase, but there are several differences between YM01-3 and AgaXa.…”

Section: Resultsmentioning

confidence: 99%

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Overexpression and Characterization of a Novel Thermostable β-Agarase YM01-3, from Marine Bacterium Catenovulum agarivorans YM01T

et al. 2014

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Genome sequencing of Catenovulum agarivorans YM01T reveals 15 open-reading frames (ORFs) encoding various agarases. In this study, extracellular proteins of YM01T were precipitated by ammonium sulfate and separated by one-dimensional gel electrophoresis. The results of in-gel agarase activity assay and mass spectrometry analysis revealed that the protein, YM01-3, was an agarase with the most evident agarolytic activity. Agarase YM01-3, encoded by the YM01-3 gene, consisted of 420 amino acids with a calculated molecular mass of 46.9 kDa and contained a glycoside hydrolase family 16 β-agarase module followed by a RICIN superfamily in the C-terminal region. The YM01-3 gene was cloned and expressed in Escherichia coli. The recombinant agarase, YM01-3, showed optimum activity at pH 6.0 and 60 °C and had a Km of 3.78 mg mL−1 for agarose and a Vmax of 1.14 × 104 U mg−1. YM01-3 hydrolyzed the β-1,4-glycosidic linkages of agarose, yielding neoagarotetraose and neoagarohexaose as the main products. Notably, YM01-3 was stable below 50 °C and retained 13% activity after incubation at 80 °C for 1 h, characteristics much different from other agarases. The present study highlights a thermostable agarase with great potential application value in industrial production.

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Section: Resultsmentioning

confidence: 99%

“…The reaction was terminated by cooling the test tube in a cold water bath. The absorbance of reducing sugar was measured at 540 nm and compared to the standard curve of d -galactose [45]. Enzyme activity (U) was defined as the amount of enzyme that liberated 1 μmol of d -galactose per minute.…”

Section: Methodsmentioning

confidence: 99%

Overexpression and Characterization of a Novel Thermostable β-Agarase YM01-3, from Marine Bacterium Catenovulum agarivorans YM01T

et al. 2014

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“…Only two α-agarases have been reported in bacteria, including Alteromonas agarilytica GJ1B (Flament et al 2007) and Thalassotalea agarivorans JAMB-A33 (Hatada et al 2006), and belong to the GH96 family. In contrast, β-agarase-producing bacteria have been reported in several taxonomically diverse genera and are found in four distinct GH families of GH16, GH50, GH86, and GH118 Dong et al 2006;Fu and Kim 2010;Henrissat 1991;Ma et al 2007;Xie et al 2013). Of these, the GH16 family is the largest family, composed of more than 3880 functionally heterogeneous members, including endogalactosidases, endoglucanases, κ-carrageenases, lichenases, and xyloglucanases etc.…”

Section: Introductionmentioning

confidence: 87%

“…cazy.org/Glycoside-Hydrolases.html). On the basis of amino acid sequence similarity, these agarases are at least classified into five distinct families of glycoside hydrolases (GHs) Dong et al 2006;Fu and Kim 2010;Henrissat 1991;Ma et al 2007;Xie et al 2013). Only two α-agarases have been reported in bacteria, including Alteromonas agarilytica GJ1B (Flament et al 2007) and Thalassotalea agarivorans JAMB-A33 (Hatada et al 2006), and belong to the GH96 family.…”

Section: Introductionmentioning

confidence: 99%

Identification and biochemical characterization of a novel endo-type β-agarase AgaW from Cohnella sp. strain LGH

Sun

Jun

et al. 2015

Appl Microbiol Biotechnol

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An agar-degrading bacterium, strain LGH, was isolated and identified as Cohnella sp. This strain had a capability of utilizing agar as a sole carbon source for growth and showed a strong agarolytic activity. A novel endo-type β-agarase gene agaW, encoding a primary translation product of 891 amino acids, including a 26 amino acid signal peptide, was cloned and identified from a genomic library of strain LGH. The AgaW belonged to the glycoside hydrolase (GH) GH50 family, with less than 39% amino acid sequence similarity with any known protein, and hydrolyzed agarose into neoagarotetraose as the major end product and neoagarobiose as the minor end product through other neoagarooligosaccharide intermediates, such as neoagarohexaose.

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“…Thus, the agaXa from Catenovulum sp. X3, a seawater bacterium, was expressed in Escherichia coli BL21 (Xie et al, 2013). The recombinant enzyme, with an estimated molecular weight of 52 kDa, was associated with the GH118 family and exhibited an optimal temperature of 52 • C ( Table 1).…”

Section: Agarasesmentioning

confidence: 99%

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes

2014

Front. Mar. Sci.

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Evidence that support the marine environment as source of useful biocatalysts for application in several areas of industry pile up, both as scientific reports or patent applications. Marine microorganisms have to endure habitats characterized by extreme conditions of salinity, temperature or pressure. Their enzymes present concomitant features, viz. thermostability or halostability, which are appealing for practical applications. The food sector is a field where enzymes are used, given their specificity, compliance with strict regulations, relatively mild operational conditions required and environmental friendly nature. The specific features presented by marine enzymes can be advantageously used both for process improvement or to develop new processes and products. In the present review the role of relevant types of enzymes for the food sector is described and recent findings on those enzymes from marine are put into context. The information provided is illustrative that in spite of the relative novelty concerning the use of marine enzymes within the scope of the food sector, some processes have reached commercial status and promising results are being obtained with several others. Moreover, there is still a vast field of resources for enzyme activity to be explored, namely since the screening process that has been considerably improved with the contribution of metagenomic libraries. It can thus be considered that future and exciting developments can be expected concerning the use of marine enzymes in the food and feed areas.

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Characterization of a novel β-agarase from an agar-degrading bacterium Catenovulum sp. X3

Cited by 61 publications

References 23 publications

Overexpression and Characterization of a Novel Thermostable β-Agarase YM01-3, from Marine Bacterium Catenovulum agarivorans YM01T

Overexpression and Characterization of a Novel Thermostable β-Agarase YM01-3, from Marine Bacterium Catenovulum agarivorans YM01T

Identification and biochemical characterization of a novel endo-type β-agarase AgaW from Cohnella sp. strain LGH

Marine enzymes and food industry: insight on existing and potential interactions

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