A comparison of lipase and trypsin encapsulated in mesoporous materials with varying pore sizes and pH conditions

Gustafsson, Hanna; Thörn, Christian; Holmberg, Krister

doi:10.1016/j.colsurfb.2011.06.012

Cited by 71 publications

(67 citation statements)

References 26 publications

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“…Many lipases, including MML and ROL, are characterized by a lid that covers the active site in solution and which exposes it when in contact with a hydrophobic surface. As discussed in our previous communication, the environment inside the pores may be favorable for activating the lipase [9]. Many of the silanol groups situated on the silica surface are lost during the calcination step, which leads to the pore walls being 390 relatively hydrophobic.…”

Section: Catalytic Activitymentioning

confidence: 99%

“…We have previously shown, for MML, that the pore size is critical for the loading capacity [9,26]. A pore size of 9 nm was found to give both high loading and good enzymatic activity while smaller pores gave both lower loading and much decreased activity.…”

Section: Relevant 270mentioning

confidence: 99%

“…shown that for Mucor miehei lipase with a molecular weight of 32 000 Da and a hydrodynamic diameter of 4.5 nm, pores with a diameter of 9 nm were optimal while for trypsin that has a molecular weight of 23 000 Da and a hydrodynamic diameter of 3.8 nm, 6 nm pores were optimal [9].…”

Section: Introductionmentioning

confidence: 99%

“…The pore dimension can be tailored with high precision by the choice of templating molecule and by the synthesis conditions [8]. The ability to tailor-make the mesoporous material with respect to pore size is attractive when the pores are used as hosts for catalysts and we [9] and others [10][11][12] have studied and determined the optimum size to house a specific enzyme. In a recent publication we have 65…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

Gustafsson

Johansson

Barrabino

et al. 2012

Colloids and Surfaces B: Biointerfaces

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Immobilization of enzymes usually improves the recyclability and stability and can sometimes also improve the activity compared to enzymes free in solution. Mesoporous silica is a widely studied material as host for immobilized enzymes because of its large internal surface area and tunable pores. It has previously been shown that the pore size is critical both for the loading capacity and for the enzymatic activity; however, less focus has been given to 20 the influence of the particle size. In this work the effect of particle size and particle morphology on the immobilization of lipase from Mucor miehei and Rhizopus oryzae have been investigated. Three kinds of mesoporous silica, all with 9 nm pores but with varying particle size (1000 nm, 300 nm and 40 nm) have been synthesized and were used as host for the lipases. The two lipases, which have the same molecular size but widely different 25 isoelectric points, were immobilized into the silica particles at varied pH values within the interval 5 to 8. The 300 nm particles were proven to be the most suitable carrier with respect to specific activity for both enzymes. The lipase from Mucor miehei was more than four times as active when immobilized at pH 8 compared to free in solution whereas the difference was less pronounced for the Rhizopus oryzae lipase. 30

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Section: Catalytic Activitymentioning

confidence: 99%

Section: Relevant 270mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

Gustafsson

Johansson

Barrabino

et al. 2012

Colloids and Surfaces B: Biointerfaces

Self Cite

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“…This technique is used to determine the amount of encapsulated protein (reviewed in 5 ), and sometimes also to monitor the kinetics of the immobilization 6 . A drawback often inherent to such indirect methods is high uncertainty and low sensitivity, and another limitation is the low time resolution that results from the time-consuming protocols for measuring protein concentration in bulk solution such as the Bradford method 7 .…”

Section: Introductionmentioning

confidence: 99%

A fluorescence spectroscopy assay for real-time monitoring of enzyme immobilization into mesoporous silica particles

Zadeh

Mallak

Carlsson

et al. 2015

Analytical Biochemistry

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Entrapping Digestive Enzymes with Engineered Mesoporous Silica Particles Reduces Metabolic Risk Factors in Humans

Waara

Iqbal

Robert‐Nicoud

et al. 2020

Adv Healthcare Materials

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Engineered mesoporous silica particles (MSP) are thermally and chemically stable porous materials composed of pure silica and have attracted attention for their potential biomedical applications. Oral intake of engineered MSP is shown to reduce body weight and adipose tissue in mice. Here, clinical data from a first‐in‐humans study in ten healthy individuals with obesity are reported, demonstrating a reduction in glycated hemoglobin (HbA1c) and low‐density lipoprotein cholesterol, which are well‐established metabolic and cardiovascular risk factors. In vitro investigations demonstrate sequestration of pancreatic α‐amylase and lipase in an MSP pore‐size dependent manner. Subsequent ex vivo experiments in conditions mimicking intestinal conditions and in vivo experiments in mice show a decrease in enzyme activity upon exposure to the engineered MSP, presumably by the same mechanism. Therefore, it is suggested that tailored MSP act by lowering the digestive enzyme availability in the small intestine, resulting in decreased digestion of macronutrient and leading to reduced caloric uptake. This novel MSP based mechanism‐of‐action, combined with its excellent safety in man, makes it a promising future agent for prevention and treatment of metabolic diseases.

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A comparison of lipase and trypsin encapsulated in mesoporous materials with varying pore sizes and pH conditions

Cited by 71 publications

References 26 publications

Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica—The effect of varied particle size and morphology

A fluorescence spectroscopy assay for real-time monitoring of enzyme immobilization into mesoporous silica particles

Entrapping Digestive Enzymes with Engineered Mesoporous Silica Particles Reduces Metabolic Risk Factors in Humans

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