Purification and characterization of a novel enzyme, alpha-neoagarooligosaccharide hydrolase (alpha-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107

Sugano, Yasushi; Kodama, Hisashi; Terada, Ichiro; Yamazaki, Yoshinari; Noma, Masana

doi:10.1128/jb.176.22.6812-6818.1994

Cited by 50 publications

(30 citation statements)

References 29 publications

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“…2, left). While many scientists have tried to investigate the α-neoagarobiose hydrolase (NABH) responsible for the reaction, only a few biochemical experiments have been able to demonstrate the activity of NABH in agarolytic microorganisms (van der Meulen and Harder 1976;Suzuki et al 2002;Day and Yaphe 1975;Sugano et al 1994). Although genetic information for NABHs is not available, NABH can be categorized into two biological classes depending on its cellular location: cytosolic NABH (Sugano et al 1994;van der Meulen and Harder 1976) and extracellular or periplasmic NABH (Suzuki et al 2002;Day and Yaphe 1975).…”

Section: Enzymology Of Agar Degradationmentioning

confidence: 98%

Agar degradation by microorganisms and agar-degrading enzymes

Chi

Chang

Hong

2012

Appl Microbiol Biotechnol

219

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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Section: Enzymology Of Agar Degradationmentioning

confidence: 98%

Agar degradation by microorganisms and agar-degrading enzymes

Chi

Chang

Hong

2012

Appl Microbiol Biotechnol

219

143

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“…to neoagarobiose, with D-galactose residues at their reducing ends (Duckworth and Turvey 1969). In some bacteria, neoagarobiose is then hydrolyzed into two monosaccharide units of 3,6-anhydro-L-galactose and D-galactose by a neoagarobiose hydrolase or a neoagarooligosaccharide hydrolase (Ha et al 2012;Hehemann et al 2012;Sugano et al 1994a). In the agarolytic pathway in marine bacterium Vibrio sp.…”

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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“…This system is capable of producing monomeric sugars from agarose and consists of ␤-agarases I and II (EC 3.2.1.81) and a neoagarooligosaccharide hydrolase (NAOS hydrolase) or a neoagarobiose hydrolase (NABH; EC 3.2.1.159), which was discovered in several agarolytic bacteria, including Saccharophagus degradans T and Zobellia galactanivorans (12,14). ␤-Agarases I and II cleave the ␤1-4 linkages of agarose to release NAOS and neoagarobiose, respectively, whereas NAOS hydrolase degrades neoagarobiose into AHG and galactose (15)(16)(17).…”

mentioning

confidence: 99%

A Novel Agarolytic β-Galactosidase Acts on Agarooligosaccharides for Complete Hydrolysis of Agarose into Monomers

Lee

Kim

Yun

et al. 2014

Appl Environ Microbiol

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cMarine red macroalgae have emerged to be renewable biomass for the production of chemicals and biofuels, because carbohydrates that form the major component of red macroalgae can be hydrolyzed into fermentable sugars. The main carbohydrate in red algae is agarose, and it is composed of D-galactose and 3,6-anhydro-L-galactose (AHG), which are alternately bonded by ␤1-4 and ␣1-3 linkages. In this study, a novel ␤-galactosidase that can act on agarooligosaccharides (AOSs) to release galactose was discovered in a marine bacterium (Vibrio sp. strain EJY3); the enzyme is annotated as Vibrio sp. EJY3 agarolytic ␤-galactosidase (VejABG). Unlike the lacZ-encoded ␤-galactosidase from Escherichia coli, VejABG does not hydrolyze common substrates like lactose and can act only on the galactose moiety at the nonreducing end of AOS. The optimum pH and temperature of VejABG on an agarotriose substrate were 7 and 35°C, respectively. Its catalytic efficiency with agarotriose was also similar to that with agaropentaose or agaroheptaose. Since agarotriose lingers as the unreacted residual oligomer in the currently available saccharification system using ␤-agarases and acid prehydrolysis, the agarotriose-hydrolyzing capability of this novel ␤-galactosidase offers an enormous advantage in the saccharification of agarose or agar in red macroalgae for its use as a biomass feedstock for fermentable sugar production.

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Purification and characterization of a novel enzyme, alpha-neoagarooligosaccharide hydrolase (alpha-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107

Cited by 50 publications

References 29 publications

Agar degradation by microorganisms and agar-degrading enzymes

Agar degradation by microorganisms and agar-degrading enzymes

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

A Novel Agarolytic β-Galactosidase Acts on Agarooligosaccharides for Complete Hydrolysis of Agarose into Monomers

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