Continuous enzymatic synthesis of lactulose in packed-bed reactor with immobilized Aspergillus oryzae β-galactosidase

Guerrero, Cecilia; Valdivia, Felipe; Ubilla, Claudia; Ramírez, Nicolás; Gómez, M.; Aburto, Carla; Vera, Carlos; Illanes, Andrés

doi:10.1016/j.biortech.2018.12.018

Cited by 37 publications

(16 citation statements)

References 43 publications

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“…The specific productivity was 3.277 g XOS g enzyme −1 h −1 in a packed‐bed reactor, leading to a robust biocatalyst that kept >90 % of its initial activity after 120 h of continuous operation . Likewise, another case study of aqueous continuous packed‐bed bioreactor (with high substrate loadings) is the lactulose syrup synthesis from fructose and lactose catalyzed by Aspergillus oryzae β‐galactosidase immobilized in glyoxyl‐agarose . The aqueous reaction media was formed by 50 % (w/w) of total initial sugars.…”

Section: Aqueous Media For Continuous Biocatalysismentioning

confidence: 99%

“…[23] Likewise, another case study of aqueous continuous packed-bed bioreactor (with high substrate loadings) is the lactulose syrup synthesis from fructose and lactose catalyzed by Aspergillus oryzae β-galactosidase immobilized in glyoxyl-agarose. [24] The aqueous reaction media was formed by 50 % (w/w) of total initial sugars. The yield of lactulose and trans-galactosylated oligosaccharides (TOS) increased at higher feed flow rates.…”

Section: Pablo Domínguez Dementioning

confidence: 99%

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Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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Enzyme catalysis (biocatalysis) is a mature strategy to perform organic synthesis with high selectivity and under mild reaction conditions. However, despite their origin and biodegradability, the simple use of enzymes is not sufficient to validate a process as green or sustainable. To reinforce the value that biocatalysis may offer, enzymatic processes can be established in environmentally‐friendly media, such as water, neoteric solvents (e. g. deep‐eutectic‐solvents, DES), biogenic solvents (e. g. 2‐MeTHF or terpenes), or even solvent‐free systems (if substrates allow that). Furthermore, these options can be conducted in continuous biocatalytic processes, which are more efficient and sustainable. Hence, a triple synergy is generated, and very promising environmentally‐friendly options can be envisaged. This conceptual paper discusses these alternatives, providing relevant, recently reported, successful examples.

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Section: Aqueous Media For Continuous Biocatalysismentioning

confidence: 99%

Section: Pablo Domínguez Dementioning

confidence: 99%

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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“…The IE can be used until a significant loss of activity is observed so optimization is needed to determine the number of cycles the enzyme can perform. Continuous mode is more advantageous since it requires fewer steps, namely the preparation of the reaction medium, transformation, recovery of the medium post-reaction, purification/removal of enzyme and obtaining of the pure product can be done simultaneously and, consequently, at lower costs (Illanes, Wilson, and Vera 2014;Guerrero et al 2019).…”

Section: Enzymatic Production Of Gos and Fos: Immobilization As A Promentioning

confidence: 99%

Recent advances in β-galactosidase and fructosyltransferase immobilization technology

Ureta

Martins

Figueira

et al. 2020

Critical Reviews in Food Science and Nutrition

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The highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: b-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes' immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of b-galactosidases and fructosyltransferases, but there is still great place for innovative developments.

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“…However, the chemical process has certain drawbacks, like the low yield attained and the formation of undesirable side products that make downstream operations for lactulose purification cumbersome and costly ( Zokaee et al, 2002 ; Aider and de Halleux, 2007 ; Panesar and Kumari, 2011 ). Within this scenario, the production of lactulose by biocatalysis using enzymes from different microbial sources is a promising alternative for making the process more in line with green chemistry principles and sustainability ( Foda and Lopez-Leiva, 2000 ; Mayer et al, 2010 ; Kim and Oh, 2012 ; Sitanggang et al, 2014 , 2015 ; Guerrero et al, 2019 ). Most of the previous research has been focused on the search and evaluation of various biocatalysts, paying little attention to optimizing the reactor configuration.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Lactulose in Continuous Stirred Tank Reactor With β-Galactosidase of Apergillus oryzae Immobilized in Monofunctional Glyoxyl Agarose Support

Ubilla

Ramírez

Valdivia

et al. 2020

Front. Bioeng. Biotechnol.

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Lactulose synthesis from fructose and lactose in continuous stirred tank (CSTR) reactor operation with glyoxyl-agarose immobilized Aspergillus oryzae β-galactosidase is reported for the first time. The effect of operational variables: inlet concentrations of sugar substrates, temperature, feed substrate molar ratio, enzyme loading and feed flow rate was studied on reactor performance. Even though the variation of each one affected to a certain extent lactulose yield (Y Lactulose ), specific productivity (π Lactulose ) and selectivity of the reaction (lactulose/transgalactosylated oligosaccharides molar ratio) (S Lu/TOS ), the most significant effects were obtained by varying the inlet concentrations of sugar substrates and the feed substrate molar ratio. Maximum Y Lactulose of 0.54 g⋅g –1 was obtained at 50°C, pH 4.5, 50% w/w inlet concentrations of sugar substrates, feed flowrate of 12 mL⋅min –1 , fructose/lactose molar ratio of 8 and reactor enzyme load of 29.06 IU H ⋅mL –1 . At such conditions S Lu/TOS was 3.7, lactose conversion (X Lactose ) was 0.39 and total transgalactosylation yield was 0.762 g⋅g –1 , meaning that 76% of the reacted lactose corresponded to transgalactosylation and 24% to hydrolysis, which is a definite advantage of this mode of operation. Even though X Lactose in CSTR was lower than in other reported modes of operation for lactulose synthesis, transgalactosylation was more favored over hydrolysis which reduced the inhibitory effect of galactose on β-galactosidase.

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Continuous enzymatic synthesis of lactulose in packed-bed reactor with immobilized Aspergillus oryzae β-galactosidase

Cited by 37 publications

References 43 publications

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Recent advances in β-galactosidase and fructosyltransferase immobilization technology

Synthesis of Lactulose in Continuous Stirred Tank Reactor With β-Galactosidase of Apergillus oryzae Immobilized in Monofunctional Glyoxyl Agarose Support

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