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Fig. 5.19
Immobilization of MP-11 in mesoporous MOFs for catalytic oxidation of 3,5-di-
tert-butylcatechol to o-quinone. Reprinted with permission from Ref. [
105
]. Copyright 2011,
American Chemical Society
reached within 30 min. The adsorption capacity for Lz and papain was as high
as 438 and 297 mg g
−
1
, respectively. Furthermore, Lz loaded on mesoporous zir-
conium phosphonates retained a structural conformation similar to its free state,
suggesting that no denaturation of Lz occurred during the adsorption process. No
leaching of Lz from the solid was observed when shaking the Lz-loaded solid in a
buffer solution. The loading of biomolecules into the porous phosphonate hybrid
networks is directly correlated with the strength of host-guest interactions [
107
],
surface area, and pore size [
105
,
106
]. Correspondingly, separation of biomole-
cules can be feasibly realized through utilizing the targeted phosphonic bridging
groups and adjusting the porosity of the phosphonate materials.
The controllable adsorption and separation of proteins are indispensable for
the application of biosensors, biocatalysts, and disease diagnostics. Size-selective
adsorption of guest protein molecules, which mainly depends on the porous prop-
erties of sorbents, has attracted tremendous research interest due to the feasibility
to adjust the porosity of the host solid materials. Although usual porous sorbents
have good capacities toward adsorbates, they still confront the predicament in sep-
arating proteins from each other. Hollow manganese phosphonate microspheres
(HMPM) with hierarchical porosity showed size selectivity toward Cytochrome
C (Cyt C, 12,400 Da, 2.6 3.2 3.3 nm
3
) and the protein bovine serum albu-
min (BSA, 66,400 Da, 5.0 7.0 7.0 nm
3
) [
108
]. The result of simultaneous
adsorption on a manganese phosphonate spherical hybrid is shown in Fig.
5.20
.
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