A facile technique to prepare cross-linked enzyme aggregates of bovine pancreatic lipase using bovine serum albumin as an additive

Cui, Jiandong; Liu, Rong Lin; Li, Lin Bo

doi:10.1007/s11814-015-0190-z

Cited by 33 publications

(28 citation statements)

References 31 publications

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“…The positive effect of soy protein may be explained by the fact that this protein provides free amino groups from lysine residues capable of increasing the number of covalent bindings between the PPL and the CLEA matrix . A more effective crosslinking achieved in the presence of additional reactive amino groups decreases the leaching of enzyme, and also increases the physical stability of the CLEA . However, higher PPL‐to‐soy protein mass ratio (1:9) decreased the global yield of the PPL‐SOY CLEAs, probably due to an increase in the CLEA size that increases the diffusional limitations …”

Section: Resultsmentioning

confidence: 99%

“…CLEA preparation is very simple, it is initialized by the protein precipitation induced by the addition of a precipitant like salts, organic solvents, or polymers, followed by the chemical crosslinking with a bifunctional or poly‐functional agent . CLEAs of several enzymes including many lipases have been reported . However, few studies about CLEAs of pancreatic lipases have been reported (Table ) .…”

Section: Introductionmentioning

confidence: 99%

“…The optimization of CLEAs includes the search of a suitable precipitant, which can keep the enzyme activity, and the search of an optimal crosslinking process that provides a physically stable particle while keeping the enzyme activity . In this sense, glutaraldehyde is the most used reagent to get the crosslinking, thanks to its very good features .…”

Section: Introductionmentioning

confidence: 99%

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1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

Ramos

Miranda

Giordano

et al. 2018

Biotechnology Progress

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The preparation of crosslinked aggregates of pancreatic porcine lipase (PPL-CLEA) was systematically studied, evaluating the influence of three precipitants and two crosslinking agents, as well as the use of soy protein as an alternative feeder protein on the catalytic properties and stability of the immobilized PPL. Standard CLEAs showed a global yield (CLEA' observed activity/offered total activity) of less than 4%, whereas with the addition of soy protein (PPL:soy protein mass ratio of 1:3) the global yield was approximately fivefold higher. The CLEA of PPL prepared with soy protein as feeder (PPL:soy protein mass ratio of 1:3) and glutaraldehyde as crosslinking reagent (10 μmol of aldehyde groups/mg of total protein) was more active mainly because of the reduced enzyme leaching in the washing step. This CLEA, named PPL-SOY-CLEA, had an immobilization yield around 60% and an expressed activity around 40%. In the ethanolysis of soybean oil, the PPL-SOY-CLEA yielded maximum fatty acid ethyl ester (FAEE) concentration around 12-fold higher than that achieved using soluble PPL (34 h reaction at 30°C, 300 rpm stirring, soybean oil/ethanol molar ratio of 1:5) with an enzyme load around 2-fold lower (very likely due to free enzyme inactivation). The operational stability of the PPL-SOY-CLEA in the ethanolysis of soybean oil in a vortex flow type reactor showed that FAEE yield was higher than 50% during ten reaction cycles of 24 h. This reactor configuration may be an attractive alternative to the conventional stirred reactors for biotransformations in industrial plants using carrier-free biocatalysts. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:910-920, 2018.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

Ramos

Miranda

Giordano

et al. 2018

Biotechnology Progress

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“…However, the activity recovery decreased with the addition of excessive amounts of glutaraldehyde. Previous reports have demonstrated that excessive glutaraldehyde might result in increasing enzyme rigidity and influence the active site availability, and therefore decrease the activity recovery of CLEAs . In contrast, the enzyme molecule may still be flexible and unstable leading to leaching in water when a small amount of glutaraldehyde is used .…”

Section: Resultsmentioning

confidence: 99%

“…Previous reports have demonstrated that excessive glutaraldehyde might result in increasing enzyme rigidity and influence the active site availability, and therefore decrease the activity recovery of CLEAs. 54,55 In contrast, the enzyme molecule may still be flexible and unstable leading to leaching in water when a small amount of glutaraldehyde is used. 56 -58 In addition, it is clear that the activity in the spherical CLEAs increased with increase of cross-linking time, and the highest activity recovery was obtained when the aggregates were cross-linked for 1.5 h ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

Cui

Lin

Feng

et al. 2017

J. Chem. Technol. Biotechnol

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BACKGROUND Cross‐linking enzyme aggregates (CLEAs) seem to be a promising immobilization method due to mild processing conditions and short preparation time. However, the CLEAs prepared in aqueous solution exhibit amorphous large clusters that cause significant mass‐transfer limitations, leading to low catalytic efficiency. In this work, novel spherical CLEAs of lipase from bovine pancreas (spherical CLEAs) were prepared within droplets dispersed in a water‐in‐hydrophobic ionic liquid microemulsion rather than a conventional aqueous solution. The properties of the spherical CLEAs were determined. RESULTS The resultant CLEAs exhibited spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs, and showed higher activity recovery (84.6%) than that of conventional CLEAs (52.8%). The high activity recovery of spherical CLEAs could be attributed to both interfacial activation of the microemulsion system and the well‐defined structure of the spherical CLEAs, which not only activated lipases in an active form, but also decreased mass‐transfer limitations. Moreover, the thermostability, storage stability, tolerance against hydrophilic solvents, and mechanical stability of the spherical CLEAs were enhanced significantly. The spherical CLEAs evidenced excellent reusability in comparison with conventional CLEAs. CONCLUSIONS The novel strategy in this study might open an attractive way towards effectively improving the catalytic properties of traditional CLEAs. © 2016 Society of Chemical Industry

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Lipases: sources, immobilization methods, and industrial applications

Gonçalves-Filho

Silva

Guidini

2019

Appl Microbiol Biotechnol

160

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A facile technique to prepare cross-linked enzyme aggregates of bovine pancreatic lipase using bovine serum albumin as an additive

Cited by 33 publications

References 31 publications

1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

Lipases: sources, immobilization methods, and industrial applications

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