Immobilization of Papain on the Mesoporous Molecular Sieve MCM-48

Zhao, Baisuo; Shi, Bo; Ma, Rui

doi:10.1002/elsc.200520094

Cited by 36 publications

(22 citation statements)

References 19 publications

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“…As listed in Table 1, the half-life (t 0.5 ) of the laccase in the Lac-PAM-CTS (4.1 h) was around 13-time longer than that of the free laccase (0.3 h), suggesting that the Lac-PAM-CTS could be stored for a long time without any significant loss in its catalytic activity. The better stability of the Lac-PAM-CTS than that of the free laccase might be attributable to the protection and cushioning effects of the supporting matrix to the external environment [37].…”

Section: Stability Of Free and Immobilized Laccasementioning

confidence: 99%

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Sun

Yang

Huang

et al. 2015

Journal of Colloid and Interface Science

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Section: Stability Of Free and Immobilized Laccasementioning

confidence: 99%

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Sun

Yang

Huang

et al. 2015

Journal of Colloid and Interface Science

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“…If not, it will adsorb only [66] --FSM-16 3-9 papain [27,117] 8. 75 3.7 3.7 5.0 MCM-41, MCM-48 4, 6.2 pepsin [73] < 1 33 kDa…”

Section: Relative Size Of the Mesopores And The Proteinmentioning

confidence: 99%

“…7.2 4.0 4.4 6.8 MCM-41, SBA-15, FSM-16, CNS 2.7-13 chloroperoxidase [65,90,93,94,106] 4.0 ca. 6.5 SBA-16, MCF, SBA-15, MCM-48, PMO-PA 3-14 manganese peroxidase [66] --FSM-16 3-9 papain [27,117] 8.75 3.7 3.7 5.0 MCM-41, MCM-48 4, 6.2 pepsin [73] < 1 33 kDa [a] CNS 13 bovine serum albumin [69][70][71]73] 4.9 5.0 7.0 7.0 CNS, MCM-41, SBA-15, Al-MCM-41 2.5-24 subtilisin [62,73] 10.4 30 kDa [a] FSM-16, CNS 2.7-13 myoglobin [71,127] 7.1 ca. 17.6 SBA-15, FDU-12, MCF 3.8-24 metmyoglobin [128] ca.…”

Section: Relative Size Of the Mesopores And The Proteinmentioning

confidence: 99%

Proteins in Mesoporous Silicates

2008

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Mesoporous silicates (MPS) have an ordered pore structure with dimensions comparable to many biological molecules. They have been extensively explored as supports for proteins and enzymes in biocatalytic applications. Since their initial discovery, novel syntheses methods have led to precise control over pore size and structure, particle size, chemical composition, and stability, thus allowing the adsorption of a wide variety of biological macromolecules, such as heme proteins, lipases, antibody fragments, and proteases, into their structures. This Review discusses the application of ordered, large-pore, functionalized mesoporous silicates to immobilize proteins for biocatalysis.

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“…7 MCM-48 is showing several applications, amongst these the utilization as enzymatic support has been studied. 8,9 Zeolites and mesoporous material synthetized with ionic liquids or molten salts at ambient temperature has been receiving attentions the last years, 10,11 due to their properties and important characteristics, making possible their application based on the principles of Green Chemistry, aiming clean chemical process and environmentally friendlies. 12 These materials act as a structure directing agent, essential reagents responsible for the formation of the material structure, making them a new option to synthesize the mesoporous material.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free

Battiston¹,

Ficanha²,

Levandoski³

et al. 2017

Quim. Nova

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publicado na web em 10/02/2017Candida antarctica lipase B (CALB) is an enzyme able to catalyze chemical reaction, however when it is used as a free enzyme, it cannot be recovered from reaction medium. One of the alternatives is to immobilize the enzymes on a support which allows the maintenance of their catalytic activities. The purpose of this paper was to immobilize the CALB on MCM-48 using the ionic solid [C 16 MI]Cl as structure director. 2 2 CCRD (Central Composite Rotational Design) was proposed to analyze the influence of the variables like enzyme mass (0.059 to 0.341 g) and ionic solid concentration (0.59 to 3.41%) in the enzyme immobilization process to obtain the maximum esterification activity in order to optimize the process. After immobilization, the study results showed that the enzymes exhibited improvement of thermal (40, 60 and 80 ºC) and storage stability (90 days), besides the possibility to reuse of the enzyme up to 10 times, showing residual activity of 50%.

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Immobilization of Papain on the Mesoporous Molecular Sieve MCM-48

Cited by 36 publications

References 19 publications

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Proteins in Mesoporous Silicates

Immobilization of lipase on mesoporous molecular sieve MCM-48 obtained using ionic solid as a structure director and esterification reaction on solvent-free

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