Development of a Bioreactor Based on Lipase Entrapped in a Monolithic Cryogel for Esterification and Interesterification Reactions

Veríssimo, Lizzy Ayra Alcântara; Mól, Paula Chequer Gouveia; Soares, Wanescy Caroliny Leite; Minim, Valéria Paula Rodrigues; Silva, Maria do Carmo Hespanhol da; Minim, Luís Antônio

doi:10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/verissimo

Cited by 11 publications

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“…Monolithic cryogels are fourth generation materials and present proven efficiency as a chromatographic matrix (Jungbauer and Hahn 2008;Mól et al, 2017;Machado et al, 2015;Gonçalves et al, 2017;Gonçalves et al, 2016;Carvalho et al, 2014;Lozinsky et al, 2003). Cryogels are versatile and can be made as column or disc-shaped, or as membranes, in addition to having a low production cost when compared to traditional chromatography matrices (Guiochon, 2007, Veríssimo et al, 2018. These matrices also have other interesting characteristics such as low load loss and flow resistance.…”

Section: Introductionmentioning

confidence: 99%

CAPTURE OF LECTINS FROM JACKFRUIT (Artocarpus integrifolia) SEEDS IN A SINGLE STEP USING A SUPERMACROPOROUS ION EXCHANGE CRYOGEL

Nascimento¹

2018

Rev.Mex.Ing.Quim.

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Section: Introductionmentioning

confidence: 99%

CAPTURE OF LECTINS FROM JACKFRUIT (Artocarpus integrifolia) SEEDS IN A SINGLE STEP USING A SUPERMACROPOROUS ION EXCHANGE CRYOGEL

Nascimento¹

2018

Rev.Mex.Ing.Quim.

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“…The sensory and nutritive values of given triglyceride also affected by these features. Several lipases catalyze a number of useful reactions such as esterification due to their activeness in organic solvents [ 47 , 53 ]. Lipases displayed pH dependent activities, generally at neutral pH 7.0 or up to pH 4.0 and 8.0 lipases are stable, Chromobacterium viscosum, A. niger and Rhizophus sp., produced extracellular lipases are active at acidic pH, and P. nitroaeducens produced alkaline lipase and active at pH 11.0 [ 54 ].…”

Section: Historical Backgroundmentioning

confidence: 99%

Microbial lipases and their industrial applications: a comprehensive review

et al. 2020

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Lipases are very versatile enzymes, and produced the attention of the several industrial processes. Lipase can be achieved from several sources, animal, vegetable, and microbiological. The uses of microbial lipase market is estimated to be USD 425.0 Million in 2018 and it is projected to reach USD 590.2 Million by 2023, growing at a CAGR of 6.8% from 2018. Microbial lipases (EC 3.1.1.3) catalyze the hydrolysis of long chain triglycerides. The microbial origins of lipase enzymes are logically dynamic and proficient also have an extensive range of industrial uses with the manufacturing of altered molecules. The unique lipase (triacylglycerol acyl hydrolase) enzymes catalyzed the hydrolysis, esterification and alcoholysis reactions. Immobilization has made the use of microbial lipases accomplish its best performance and hence suitable for several reactions and need to enhance aroma to the immobilization processes. Immobilized enzymes depend on the immobilization technique and the carrier type. The choice of the carrier concerns usually the biocompatibility, chemical and thermal stability, and insolubility under reaction conditions, capability of easy rejuvenation and reusability, as well as cost proficiency. Bacillus spp., Achromobacter spp., Alcaligenes spp., Arthrobacter spp., Pseudomonos spp., of bacteria and Penicillium spp., Fusarium spp., Aspergillus spp., of fungi are screened large scale for lipase production. Lipases as multipurpose biological catalyst has given a favorable vision in meeting the needs for several industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. This review represents a discussion on microbial sources of lipases, immobilization methods increased productivity at market profitability and reduce logistical liability on the environment and user.

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“…Above this concentration, a decrease in activity was observed when compared to the control (without the addition of Triton X-100). According to Veríssimo et al, 33 lipases tend to form aggregates in solution that can negatively affect the enzyme activity. The addition of a surfactant can promote the breakdown of these aggregates, stabilizing them in their most active conformation (open form), and thereby increasing their activity.…”

Section: Lipase Immobilization By Adsorption Effect Of the Initial Ph Of The Lipase Solution On The Immobilization Processmentioning

confidence: 99%

“…These aggregate are formed via specific interactions between the open forms of two lipase molecules (lipase-lipase dimers). [30][31][32] According to Veríssimo et al, 33 and Oliveira et al, 34 the addition of surfactants in the dilution medium can inhibit the formation of these aggregates, stabilizing the enzyme in its open form and causing an increase in catalytic activity.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of activated carbon from hydrothermally carbonized tamarind seeds for lipase immobilization: characterization and application in aroma ester synthesis

Gonçalves

Gandolfi

Bonomo

et al. 2021

J of Chemical Tech & Biotech

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BACKGROUND: This study aimed to evaluate the effect of hydrothermal carbonization on the activated carbons properties of tamarind seeds, which were used as a support in porcine pancreatic lipase (PPL) immobilization, and to evaluate the biocatalyst in the butyl butyrate synthesis. RESULTS:The activated carbon from hydrochar (ACHT) had oxygen functional groups content about 32.5% higher and a lower point of zero charge (4.42) when compared to those obtained from crude bran (ACT). Differences in textural properties were also observed, with an average pore diameter of 3.20 and 6.46 nm for ACHT and ACT, respectively. The optimal immobilization pH was 5.0, resulting in enzyme loading of 71.8 ± 1.42 mg.g 1 and 53.03 ± 0.31 mg•g −1 , and in a hydrolytic activity of 222.47 ± 2.80 U•g −1 and 257.18 ± 7.31 U•g −1 for ACT and ACHT, respectively. The addition of Triton X-100 0.025 w•v −1 to the immobilization buffer led to an increase in ∼7% of the hydrolytic activity. The PPL immobilized in pH 5.0 was used in the butyl butyrate synthesis, using a mixture of butanol (240 mmol L −1 ) and butyric acid (120 mmol L −1 ), with an esterification yield of ±83% after 4 h of reaction at 40 °C. CONCLUSION:The PPL immobilized on ACHT showed a small decrease in activity over time, with a residual esterification yield of 84% after 4 cycles of reuse. The present results suggest that the supported biocatalyst has the potential to be used in aqueous and organic media, such as hydrolytic lipid reactions and aroma synthesis mostly used in the food industry.

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Development of a Bioreactor Based on Lipase Entrapped in a Monolithic Cryogel for Esterification and Interesterification Reactions

Cited by 11 publications

References 0 publications

CAPTURE OF LECTINS FROM JACKFRUIT (Artocarpus integrifolia) SEEDS IN A SINGLE STEP USING A SUPERMACROPOROUS ION EXCHANGE CRYOGEL

CAPTURE OF LECTINS FROM JACKFRUIT (Artocarpus integrifolia) SEEDS IN A SINGLE STEP USING A SUPERMACROPOROUS ION EXCHANGE CRYOGEL

Microbial lipases and their industrial applications: a comprehensive review

Synthesis of activated carbon from hydrothermally carbonized tamarind seeds for lipase immobilization: characterization and application in aroma ester synthesis

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