Recombinant agarase increases the production of reducing sugars from HCl-treated Gracilaria verrucosa, a red algae

Kim, Se Won; Kim, Yong-Woon; Hong, Chae-Hwan; Lyo, Inwoong; Lim, Ho-Dong; Kim, Geun-Joong; Shin, Hyun‐Jae

doi:10.1016/j.algal.2017.01.008

Cited by 24 publications

(11 citation statements)

References 27 publications

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“…Recombinant β-agarase (Aga 50A) from Escherichia coli hydrolyzes the Gracilaria spp. agar to produce higher amounts of AOS than commercial agarase [ 44 ]. Cui et al isolated a novel β-agarase from the marine bacterium, Catenovulum agarivorans YM01T, that could hydrolyze the β-1,4-glycosidic linkages of agar, and obtained neoagarotetraose and neoagarohexaose as the main products.…”

Section: Production Of Oligosaccharide From Red Seaweedmentioning

confidence: 99%

Oligosaccharides Derived from Red Seaweed: Production, Properties, and Potential Health and Cosmetic Applications

et al. 2018

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Because of their potential use as functional ingredients in human nutrition, oligosaccharides derived from natural sources are receiving paramount consideration. Red seaweed, a proven rich source of agar and carrageenan, is one of the most abundantly present sources of such oligosaccharides. Agaro-oligosaccharides (AOS) and carrageenan-oligosaccharides (COS) are produced from agar and carrageenan, respectively, through chemical and enzymatic hydrolyses. Enzymatic hydrolysis of agar and carrageenan into oligosaccharides is preferred in industrial production because of certain problems associated with chemical hydrolysis, including the release of high amounts of monosaccharides and undesirable toxic products, such as furfural. AOS and COS possess many biological activities, including prebiotic, immuno-modulatory, anti-oxidant, and anti-tumor activities. These activities are related to their chemical structure, molecular weight, degree of polymerization, and the flexibility of the glycosidic linkages. Therefore, the structure–function relationship and the mechanisms occurring during the specific biological applications of AOS and COS are discussed herein. Moreover, the chromatographic separation, purification, and characterization of AOS and COS are also part of this review. This piece of writing strives to create a new perspective on the potential applications of AOS and COS in the functional food and pharmaceutical industry.

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Section: Production Of Oligosaccharide From Red Seaweedmentioning

confidence: 99%

Oligosaccharides Derived from Red Seaweed: Production, Properties, and Potential Health and Cosmetic Applications

et al. 2018

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“…For the production of reducing sugars from Gracilaria verrucosa, red algae, about three recombinant agarase genes corresponding Aga50A, Aga50D, and NABH, which belonged to endotype GH118 family were cloned into E. coli from Saccharophagus degradans 2-40. The molecular weights of these recombinant agarases Aga50A, Aga50D, and NABH were 87.8 kDa, 89.7 kDa, and 44.0 kDa respectively (Kim et al 2018). From a different host system, other than E. coli, an endotype β-agarase of GH118 family was documented.…”

Section: Molecular Characteristics Of the Recombinant β-Agarasesmentioning

confidence: 96%

“…Fresh seaweed 6 30 6-7 20-30 °C Liu et al (2014b) degraded into NA4 and NA2 (Jung et al 2017). The simple agar oligosaccharide neoagarobiose (NA2) was obtained as the only degradation product by the action of three enzymes: Aga50A, Aga50D, and NABH (neoagarobiose Hydrolase) in a systematic fashion and the specific activities of these enzymes were 11.96, 13.18, and 10.25 U/mg, respectively (Kim et al 2018). Upon action of AgWH50C and Aga50D on agarose, they both yielded neoagarobiose (NA2) as the degradation product (Liu et al 2014b;Kim et al 2010).…”

Section: Agwh50cmentioning

confidence: 99%

“…The recombinant β-agarases belong to the glycoside hydrolase (GH) family such as GH16, GH39, GH50, GH86, and GH118. Predominantly, the recombinant β-agarases were from marine microbes and their genera include Agarivorans (Liu et al 2014a, b;Lee et al 2012;Lin et al 2012), Alteromonas (Seo et al 2014;Chi et al 2014), Aquimarina (Lin et al 2017), Catenovulum (An et al 2018;Cui et al 2014;Xie et al 2013), Cellulophaga (Ramos et al 2018), Flammeovirga (Dong et al 2016;Hou et al 2015;Yang et al 2011;Chen et al 2016;Di et al 2018), Gayadomonas (Lee et al 2018;Jung et al 2017a, b), Microbulbifer (Su et al 2017), Micrococcaceae (Xu et al 2018), Pseudoalteromonas (Chi et al 2015a, b;Oh et al 2010a, b), Pseudomonas (Hsu et al 2015), Saccharophagus (Kim et al 2010(Kim et al , 2017(Kim et al , 2018Lee et al 2013), Simiduia (Tawara et al 2015), Thalassomonas (Liang et al 2014), and Vibrio (Liao et al 2011) whereas few were from soil bacteria Streptomyces (Temuujin et al 2011(Temuujin et al , 2012, Cohnella (Li et al 2015) and one exclusive source was the activated sludges of sewage plant from which Cellvibrio (Osamu et al 2012) had been identified with agarolytic property.…”

Section: Introductionmentioning

confidence: 99%

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Recombinant β-agarases: insights into molecular, biochemical, and physiochemical characteristics

Veerakumar

Manian

2018

3 Biotech

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Agarases (agarose 4-glycanohydrolase; EC 3.2.1.81) are class of enzymes that belong to glycoside hydrolase (GH) family capable of hydrolyzing agar. Their classification depends on hydrolysis pattern and product formation. Among all the agarases, β-agarases and the oligosaccharides formed by its action have fascinated quite a lot of industries. Ample of β-agarase genes have been endowed from marine sources such as algae, sea water, and marine sediments, and the expression of these genes into suitable host gives rise to recombinant β-agarases. These recombinant β-agarases have wide range of industrial applications due to its improved catalytic efficiency and stability in tough environments with ease of production on large scale. In this review, we have perused different types of recombinant β-agarases in consort with their molecular, physiochemical, and kinetic properties in detail and the significant features of those agarases are spotlighted. From the literature reviewed after 2010, we have found that the recombinant β-agarases belonged to the families GH16, GH39, GH50, GH86, and GH118. Among that, GH39, GH50, and GH86 belonged to clan GH-A, while the GH16 family belonged to clan GH-B. It was observed that GH16 is the largest polyspecific glycoside hydrolase family with ample number of β-agarases and the families GH50 and GH118 were found to be monospecific with only β-agarase activity. And, out of 84 non-catalytic carbohydrate-binding modules (CBMs), only CBM6 and CBM13 were professed in β-agarases. We witnessed a larger heterogeneity in molecular, physiochemical, and catalytic characteristics of the recombinant β-agarases including molecular mass: 32-132 kDa, optimum pH: 4.5-9, optimum temperature 16-60 °C, K M : 0.68-59.8 mg/ml, and V max : 0.781-11,400 U/ mg. Owing to this extensive range of heterogeneity, they have lion's share in the multibillion dollar enzyme market. This review provides a holistic insight to a few aspects of recombinant β-agarases which can be referred by the upcoming explorers to this area.

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“…Different articles found have a more practically oriented nature, reporting applications of already known activities. A combined acid and enzymatic hydrolysis using a recombinant agarase to produce total reducing sugars from Gracilaria verrucosa was published [ 34 ]. A 5% increase (47.4%) with respect to the previous value of reducing sugars obtained by commercial enzyme is claimed for this biorefinery-oriented application.…”

Section: General Analysis Of Reference Materialsmentioning

confidence: 99%

Update on Marine Carbohydrate Hydrolyzing Enzymes: Biotechnological Applications

Trincone

2018

Molecules

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After generating much interest in the past as an aid in solving structural problems for complex molecules such as polysaccharides, carbohydrate-hydrolyzing enzymes of marine origin still appear as interesting biocatalysts for a range of useful applications in strong interdisciplinary fields such as green chemistry and similar domains. The multifaceted fields in which these enzymes are of interest and the scarce number of original articles in literature prompted us to provide the specialized analysis here reported. General considerations from modern (2016–2017 interval time) review articles are at start of this manuscript; then it is subsequently organized in sections according to particular biopolymers and original research articles are discussed. Literature sources like the Science Direct database with an optimized W/in search, and the Espacenet patent database were used.

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Recombinant agarase increases the production of reducing sugars from HCl-treated Gracilaria verrucosa, a red algae

Cited by 24 publications

References 27 publications

Oligosaccharides Derived from Red Seaweed: Production, Properties, and Potential Health and Cosmetic Applications

Oligosaccharides Derived from Red Seaweed: Production, Properties, and Potential Health and Cosmetic Applications

Recombinant β-agarases: insights into molecular, biochemical, and physiochemical characteristics

Update on Marine Carbohydrate Hydrolyzing Enzymes: Biotechnological Applications

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