Agarose hydrolysis by two-stage enzymatic process and bioethanol production from the hydrolysate

Seo, Young Bin; Park, Juyi; Huh, In Young; Hong, Soon-Kwang; Chang, Yong Keun

doi:10.1016/j.procbio.2016.03.011

Cited by 16 publications

(8 citation statements)

References 18 publications

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“…20−22 High-titer production of L-AHG is largely hampered by low agarose or agar loadings due to the insolubility of agarose or agar in water. 11 To date, loadings of agarose have remained at less than 15% (w/v) in hydrolysis reactions 13,14,16 (Table 1). Therefore, it is necessary to develop a new saccharification process that is suitable for high loadings of agarose for the industrial saccharification of agar or red macroalgae.…”

Section: Resultsmentioning

confidence: 99%

“…In this process, agarose is depolymerized into neoagarobiose (NAB) by endo-and exotype β-agarases, and NAB is then hydrolyzed intoL-AHG and D-Gal by α-neoagarobiose hydrolase (α-NABH). 11 The advantage of the enzymatic saccharification process is high L-AHG yields that can be obtained by complete hydrolysis of agarose due to the high substrate specificity of those enzymes. However, because agarose is insoluble in water at most temperatures other than in boiling water, only low loadings of agarose can be applied to the enzymatic saccharification process, 12 thus resulting in low L-AHG titers after enzymatic saccharification.…”

Section: Introductionmentioning

confidence: 99%

“…The second type is the enzymatic saccharification process. In this process, agarose is depolymerized into neoagarobiose (NAB) by endo- and exotype β-agarases, and NAB is then hydrolyzed into l -AHG and d -Gal by α-neoagarobiose hydrolase (α-NABH) . The advantage of the enzymatic saccharification process is high l -AHG yields that can be obtained by complete hydrolysis of agarose due to the high substrate specificity of those enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Novel Two-Step Process Utilizing a Single Enzyme for the Production of High-Titer 3,6-Anhydro-l-galactose from Agarose Derived from Red Macroalgae

Kim

Yun

Lee

et al. 2018

J. Agric. Food Chem.

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Anhydro-L-galactose (L-AHG), a major component of agarose derived from red macroalgae, has excellent potential for industrial applications based on its physiological activities such as skin whitening, moisturizing, anticariogenicity, and anti-inflammation. However, L-AHG is not yet commercially available due to the complexity, inefficiency, and high cost of the current processes for producing L-AHG. Currently, L-AHG production depends on a multistep process requiring several enzymes. Here, we designed and tested a novel two-step process for obtaining high-titer L-AHG by using a single enzyme. First, to depolymerize agarose preferentially into agarobiose (AB) at a high titer, the agarose prehydrolysis using phosphoric acid as a catalyst was optimized at a 30.7% (w/v) agarose loading, which is the highest agarose or agar loading reported so far. Then AB produced by the prehydrolysis was hydrolyzed into L-AHG and D-galactose (D-Gal) by using a recently discovered enzyme, Bgl1B. We suggest that this simple and efficient process could be a feasible solution for the commercialization and mass production of L-AHG.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Novel Two-Step Process Utilizing a Single Enzyme for the Production of High-Titer 3,6-Anhydro-l-galactose from Agarose Derived from Red Macroalgae

Kim

Yun

Lee

et al. 2018

J. Agric. Food Chem.

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“…The idea here is to depict both the state of the art about marine enzyme-based bioprocesses and the importance of marine-originating feedstocks in biorefinery. Therefore, biocatalysts and biomass are the two fundamental elements on which the analysis of primary articles in the literature is based here ( Table 1 [ 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 ]). The selected articles inserted in Table 1 deal with (i) cellulases and other important carbohydrate-active enzymes; (ii) lipases, to manipulate feedstock oils for biodiesel production and (iii) other biocatalysts, including those commercially available.…”

Section: Biorefinerymentioning

confidence: 99%

Enzymatic Processes in Marine Biotechnology

Trincone

2017

Marine Drugs

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In previous review articles the attention of the biocatalytically oriented scientific community towards the marine environment as a source of biocatalysts focused on the habitat-related properties of marine enzymes. Updates have already appeared in the literature, including marine examples of oxidoreductases, hydrolases, transferases, isomerases, ligases, and lyases ready for food and pharmaceutical applications. Here a new approach for searching the literature and presenting a more refined analysis is adopted with respect to previous surveys, centering the attention on the enzymatic process rather than on a single novel activity. Fields of applications are easily individuated: (i) the biorefinery value-chain, where the provision of biomass is one of the most important aspects, with aquaculture as the prominent sector; (ii) the food industry, where the interest in the marine domain is similarly developed to deal with the enzymatic procedures adopted in food manipulation; (iii) the selective and easy extraction/modification of structurally complex marine molecules, where enzymatic treatments are a recognized tool to improve efficiency and selectivity; and (iv) marine biomarkers and derived applications (bioremediation) in pollution monitoring are also included in that these studies could be of high significance for the appreciation of marine bioprocesses.

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“…However, production of some byproducts is still unavoidable . Neoagarobiose hydrolysis is beneficial for increasing ethanol production by fermenting both l -AHG and galactose. , However, it is not conducive for the preparation of l -AHG with high purity because of the difficulty in separating the two monosaccharides. In the same group, Yun et al also reported that l -AHG was obtained from agarose by β-agarases I and II and NABH sequentially.…”

Section: Introductionmentioning

confidence: 99%

Coimmobilization of β-Agarase and α-Neoagarobiose Hydrolase for Enhancing the Production of 3,6-Anhydro-l-galactose

Wang

Sun

Liu

et al. 2018

J. Agric. Food Chem.

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Here we report a simple and efficient method to produce 3,6-anhydro-l-galactose (l-AHG) and agarotriose (AO3) in one step by a multienzyme system with the coimmobilized β-agarase AgWH50B and α-neoagarobiose hydrolase K134D. K134D was obtained by AgaWH117 mutagenesis and showed improved thermal stability when immobilized via covalent bonds on functionalized magnetic nanoparticles. The obtained multienzyme biocatalyst was characterized by Fourier transform infrared spectroscopy (FTIR). Compared with free agarases, the coimmobilized agarases exhibited a relatively higher agarose-to-l-AHG conversion efficiency. The yield of l-AHG obtained with the coimmobilized agarases was 40.6%, which was 6.5% higher than that obtained with free agarases. After eight cycles, the multienzyme biocatalyst still preserved 46.4% of the initial activity. To the best of our knowledge, this is the first report where two different agarases were coimmobilized. These results demonstrated the feasibility of the new method to fabricate a new multienzyme system onto magnetic nanoparticles via covalent bonds to produce l-AHG.

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Agarose hydrolysis by two-stage enzymatic process and bioethanol production from the hydrolysate

Cited by 16 publications

References 18 publications

Novel Two-Step Process Utilizing a Single Enzyme for the Production of High-Titer 3,6-Anhydro-l-galactose from Agarose Derived from Red Macroalgae

Novel Two-Step Process Utilizing a Single Enzyme for the Production of High-Titer 3,6-Anhydro-l-galactose from Agarose Derived from Red Macroalgae

Enzymatic Processes in Marine Biotechnology

Coimmobilization of β-Agarase and α-Neoagarobiose Hydrolase for Enhancing the Production of 3,6-Anhydro-l-galactose

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