Characterization of a Novel Neoagarobiose-Producing GH42 β-Agarase, AgaJ10, from Gayadomonas joobiniege G7

Choi, Umji; Jung, Subin; Hong, Soon-Kwang; Lee, Chang-Ro

doi:10.1007/s12010-019-02992-5

Cited by 11 publications

(6 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the present investigation, the substrate specificity assessment suggests that partially purified agarase belongs to β-agarase that produces neoagarooligosaccharides from agar. These findings are consistent with the results of several recent studies dealing with agarases from various sources, describing the cleavage of β-bonds in agar and agarose (Han et al, 2019b;Li et al, 2019b;Choi et al, 2019;Chen et al, 2019b). Agarases are characterized as α-agarases and β-agarases according to the cleavage pattern.…”

Section: Discussionsupporting

confidence: 92%

“…Agarases are characterized as α-agarases and β-agarases according to the cleavage pattern. Li et al, (2018);Hafizah et al, (2019);Liu et al, (2019);Lee et al, (2019) revealed that the basic products of the α-agarases and β-agarases are agarobiose and neoagarobiose, respectively. Results of this study revealed the significant anti-oxidant potential of the NAOs produced by hydrolysis of agar using βagarases derived from A. agarilytica NI125.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Enhanced anti-oxidant activity of neoagarooligosaccharides produced by β-agarase derived from Aquimarina agarilytica NI125

Farahat

2019

Novel Research in Microbiology Journal

View full text Add to dashboard Cite

The neoagarooligosaccharides have received growing attention owing to their physiological activities. The aim of this study was the isolation of agarase-producing bacteria for production of agar hydrolysates with special emphasis on their anti-oxidant potential. An agarolytic strain NI125 was isolated from Nelson's Island, Alexandria, Egypt. Based on 16S rRNA analysis and extensive phenotypic characterization, it was identified as Aquimarina agarilytica. Maximum enzyme production was achieved after 24 h incubation at 20°C, and tryptone was recorded to be the best nitrogen source for agarase production. Extracellular agarase was partially purified by ammonium sulfate precipitation. The substrate specificity assay using p-nitrophenyl-α/β-D-galactopyranoside revealed the cleavage of the β-linkage rather than the α-linkage. Neoagarooligosaccharides produced by the partially purified β-agarase expressed promising anti-oxidant properties, with 23% free radical scavenging potential. Notable enhancement of the anti-oxidant potency of the oligosaccharides was achieved (up to 87% scavenging ability) by sulfation of the agar prior to hydrolysis for 12 h with β-agarase. Results obtained suggest the potential application of the produced neoagarooligosaccharides anti-oxidants as promising additives in food and feed products.

show abstract

Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Enhanced anti-oxidant activity of neoagarooligosaccharides produced by β-agarase derived from Aquimarina agarilytica NI125

Farahat

2019

Novel Research in Microbiology Journal

View full text Add to dashboard Cite

show abstract

“…These agarases were variously sorted into the GH39, GH42, and GH86 families. In detail, AgaJ5 possesses a prominent cold tolerance, as it retained enzymatic activity of 40% at 10 °C [ 13 ]; AgaJ9 sustained 89% of agarase activity at 10 °C [ 8 ]; AgaJ10 showed 50% of enzymatic activity at 10 °C [ 9 ]; whereas Aga21 retained 85% of enzymatic activity at 10 °C [ 14 ]. Nevertheless, the agarases that can work at 0 °C are rarely reported.…”

Section: Discussionmentioning

confidence: 99%

“…Compared to α-agarases, β-agarases have a wider distribution in nature [ 7 ]. β-agarases belong to glycoside hydrolase (GH) families, including GH 16, GH 39, GH 42, GH 50, GH 86, and GH118 [ 2 , 8 , 9 ]. Neoagarobiose (NA2), neoagarotetraose (NA4), neoagarohexaose (NA6), neoagarooctaose (NA8), neoagarodecaose (NA10), and neoagarododecaose (NA12) are the usual products of β-agarases [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Expression and Characterization of a Novel Cold-Adapted and Stable β-Agarase Gene agaW1540 from the Deep-Sea Bacterium Shewanella sp. WPAGA9

Wang

Yan

et al. 2021

Marine Drugs

View full text Add to dashboard Cite

The neoagaro-oligosaccharides, degraded from agarose by agarases, are important natural substances with many bioactivities. In this study, a novel agarase gene, agaW1540, from the genome of a deep-sea bacterium Shewanella sp. WPAGA9, was expressed, and the recombinant AgaW1540 (rAgaW1540) displayed the maximum activity under the optimal pH and temperature of 7.0 and 35 °C, respectively. rAgaW1540 retained 85.4% of its maximum activity at 0 °C and retained more than 92% of its maximum activity at the temperature range of 20–40 °C and the pH range of 4.0–9.0, respectively, indicating its extensive working temperature and pH values. The activity of rAgaW1540 was dramatically suppressed by Cu2+ and Zn2+, whereas Fe2+ displayed an intensification of enzymatic activity. The Km and Vmax of rAgaW1540 for agarose degradation were 15.7 mg/mL and 23.4 U/mg, respectively. rAgaW1540 retained 94.7%, 97.9%, and 42.4% of its maximum activity after incubation at 20 °C, 25 °C, and 30 °C for 60 min, respectively. Thin-layer chromatography and ion chromatography analyses verified that rAgaW1540 is an endo-acting β-agarase that degrades agarose into neoagarotetraose and neoagarohexaose as the main products. The wide variety of working conditions and stable activity at room temperatures make rAgaW1540an appropriate bio-tool for further industrial production of neoagaro-oligosaccharides.

show abstract

“…In addition, agar can be used as a supporting material for enzyme or bacterial immobilization to enhance the stability of the system, which allows long-term operation [ 6 , 7 ]. Agar can also be used to manufacture biodegradable polymers, such as bioplastics [ 8 ], and can be used in wet-fiber [ 9 ], eco-friendly biocleaning processes [ 10 ] as well as in medical treatments, such as microencapsulation [ 11 ], drug delivery [ 12 ], and bone generation [ 13 ]. In this sense, agar is expected to be widely used in the food and chemical industry as well as in the medical field.…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7

Seo¹,

Tsevelkhorloo²,

Lee³

et al. 2020

J. Microbiol. Biotechnol.

Self Cite

View full text Add to dashboard Cite

Agarose is a major constituent of agar, the main component of red algal biomass. Agar is a heterogeneous hydrophilic colloidal polysaccharide composed of alternately linked 3-O-linked β-D-galactopyranose (G) and 4-O-linked α-L-galactopyranose (L) [1, 2]. Agarose is a main component of agar, where L is substituted with 3,6-anhydro-L-galactose (L-AHG), forming a linear polymer with an average molecular mass of 120,000 Da [3]. Agar has been used as a dietary food and gelling agent for a long time in many Asian countries and has been generally recognized as safe by the United States Food and Drug Administration. Owing to the unique properties of thermal hysteresis in the sol-to-gel transition and its structural stability, agar has been widely used in bacterial plate culture as well as in electrophoretic and chromatographic supporting materials [4]. Recently, marine algal biomass has been highlighted in many studies because it is a valuable and sustainable resource that can substitute fossil-based chemical feed stocks, including petroleum [5]. In addition, agar can be used as a supporting material for enzyme or bacterial immobilization to enhance the stability of the system, which allows long-term operation [6, 7]. Agar can also be used to manufacture biodegradable polymers, such as bioplastics [8], and can be used in wet-fiber [9], eco-friendly biocleaning processes [10] as well as in medical treatments, such as microencapsulation [11], drug delivery [12], and bone generation [13]. In this sense, agar is expected to be widely used in the food and chemical industry as well as in the medical field. Agar can be degraded by chemical treatments or enzymatic hydrolysis for industrial applications. Because the 1,3-α-3,6-anhydro-L-galactosidase (α-neoagarooligosaccharide hydrolase) catalyzes the last step of agar degradation by hydrolyzing neoagarobiose into monomers, D-galactose, and 3,6-anhydro-Lgalactose, which is important for the bioindustrial application of algal biomass. Ahg943, from the agarolytic marine bacterium Gayadomonas joobiniege G7, is composed of 423 amino acids (47.96 kDa), including a 22-amino acid signal peptide. It was found to have 67% identity with the α-neoagarooligosaccharide hydrolase ZgAhgA, from Zobellia galactanivorans, but low identity (< 40%) with the other α-neoagarooligosaccharide hydrolases reported. The recombinant Ahg943 (rAhg943, 47.89 kDa), purified from Escherichia coli, was estimated to be a monomer upon gel filtration chromatography, making it quite distinct from other α-neoagarooligosaccharide hydrolases. The rAhg943 hydrolyzed neoagarobiose, neoagarotetraose, and neoagarohexaose into D-galactose, neoagarotriose, and neoagaropentaose, respectively, with a common product, 3,6anhydro-L-galactose, indicating that it is an exo-acting α-neoagarooligosaccharide hydrolase that releases 3,6-anhydro-L-galactose by hydrolyzing α-1,3 glycosidic bonds from the nonreducing ends of neoagarooligosaccharides. The optimum pH and temperature of Ahg943 activity were 6.0 and 20°C, respectively. In parti...

show abstract

Characterization of a Novel Neoagarobiose-Producing GH42 β-Agarase, AgaJ10, from Gayadomonas joobiniege G7

Cited by 11 publications

References 30 publications

Enhanced anti-oxidant activity of neoagarooligosaccharides produced by β-agarase derived from Aquimarina agarilytica NI125

Enhanced anti-oxidant activity of neoagarooligosaccharides produced by β-agarase derived from Aquimarina agarilytica NI125

Expression and Characterization of a Novel Cold-Adapted and Stable β-Agarase Gene agaW1540 from the Deep-Sea Bacterium Shewanella sp. WPAGA9

Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7

Contact Info

Product

Resources

About