Purification and characterization of cold-adapted beta-agarase from an Antarctic psychrophilic strain

Li, Jiang; Hu, Q.Y.; Li, Yuquan; Xu, Yifeng

doi:10.1590/s1517-838246320131289

Cited by 12 publications

(5 citation statements)

References 31 publications

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“…Aga1 is an exo-type β-agarase, which hydrolyses agarose into NA 4 and NA 6 as end products. In contrast, most exo-agarases produce only one type of oligosaccharide instead of a mixture; for example, Aga50D 37 , Aga21 38 , and AgWH50A 15 produce NA2 as an end product, and AgWH50C 14 produces NA4 as an end product. The structure of agarase greatly affects its end products 39 .…”

Section: Discussionmentioning

confidence: 99%

Horizontal Transfer of a Novel Soil Agarase Gene from Marine Bacteria to Soil Bacteria via Human Microbiota

Song

Wei

et al. 2016

Sci Rep

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Seaweed is receiving an increasing amount of attention as a “sea vegetable”. The microbiota of coastal populations may acquire seaweed associated enzymes through marine food. Several agarases have been found in non-marine environments; however, their origin is unknown. In this study, a hypothetical protein, Aga1, was identified as an agarase from an inland soil agar-degrading bacterium, Paenibacillus sp. SSG-1.Having low similarity to known glycoside hydrolases, Aga1 may be a distant member of the glycoside hydrolase family 86. Aga1 has good pH stability (pH 3–11) and is stable in the presence of various metal ions. Aga1 is an exo-type β-agarase that produces NA 4 (neoagarotetraose) and NA 6 (neoagarohexaose) as its main products. In addition, Aga1 may be a cell-surface-binding protein. The bioinformatic analysis showed aga1 may have been transfered together with its surrounding genes, from marine bacteria to soil bacteria via human microbiota. The use of seaweed as food and the disposal of human faeces or saliva were the most likely reasons for this gene transfer pathway. Notably, the results also indicated that microbes from inland humans may degrade agar and that these microbes may have acquired seaweed associated genes because of increased seaweed in diets.

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Section: Discussionmentioning

confidence: 99%

Horizontal Transfer of a Novel Soil Agarase Gene from Marine Bacteria to Soil Bacteria via Human Microbiota

Song

Wei

et al. 2016

Sci Rep

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“…AgaDL6 depolymerizes agarose into NA4 and NA6 as final products. This is distinct from most exo-agarases, which produce only one type of oligosaccharide as the final product [44,45]. The primary structure of the agarase determines its function and will ultimately affect its final products.…”

Section: Discussionmentioning

confidence: 98%

Isolation and Characterization of an Eosinophilic GH 16 ��-Agarase (AgaDL6) from an Agar-Degrading Marine Bacterium Flammeovirga sp. HQM9

Liu¹,

Tian²,

Peng³

et al. 2019

Journal of Microbiology and Biotechnology

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A special eosinophilic agarase exo-type β-agarase gene, AgaDL6, was cloned from a marine agar-degrading bacterium, Flammeovirga sp. HQM9. The gene comprised 1,383-bp nucleotides encoding a putative agarase AgaDL6 of 461 amino acids with a calculated molecular mass of 52.8 kDa. Sequence analysis revealed a β-agarase domain that belongs to the glycoside hydrolase family (GH) 16 and a carbohydrate-binding module (CBM_4_9) unique to agarases. AgaDL6 was heterologously expressed in Escherichia coli BL21 (DE3). Enzyme activity analysis of the purified protein showed that the optimal temperature and pH of AgaDL6 were 50°C and 3.0, respectively. AgaDL6 showed thermal stability by retaining more than 98% of activity after incubation for 2 h at 50°C, a feature quite different from other agarases. AgaDL6 also exhibited outstanding acid stability, retaining 100% of activity after incubation for 24 h at pH 2.0 to 5.0, a property distinct from other agarases. This is the first agarase characterized to have such high acid stability. In addition, we observed no obvious stimulation or inhibition of AgaDL6 in the presence of various metal ions and denaturants. AgaDL6 is an exo-type β-1,4 agarase that cleaved agarose into neoagarotetraose and neoagarohexaose as the final products. These characteristics make AgaDL6 a potentially valuable enzyme in the cosmetic, food, and pharmaceutical industries.

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“…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%

“…In detail, AgaJ5 retained ~40% of the maximum enzymatic activity at 10 °C [ 13 ]. AgaJ9 maintained more than 80% of the maximum activity at 5 °C [ 8 ], and Aga21 retained as much as 85% of the maximum activity at 10 °C [ 14 ]. However, the agarases that can work at extreme temperatures, such as 0 °C, are rarely reported.…”

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

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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.

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Purification and characterization of cold-adapted beta-agarase from an Antarctic psychrophilic strain

Cited by 12 publications

References 31 publications

Horizontal Transfer of a Novel Soil Agarase Gene from Marine Bacteria to Soil Bacteria via Human Microbiota

Horizontal Transfer of a Novel Soil Agarase Gene from Marine Bacteria to Soil Bacteria via Human Microbiota

Isolation and Characterization of an Eosinophilic GH 16 ��-Agarase (AgaDL6) from an Agar-Degrading Marine Bacterium Flammeovirga sp. HQM9

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

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