Metal-organic frameworks as novel matrices for efficient enzyme immobilization: An update review

Enzyme embedded metal organic framework (enzyme-MOF): De novo approaches for immobilization.

Immobilization of proline activated lipase within metal organic framework (MOF).

Recent advances in enzyme immobilization based on novel porous framework materials and its applications in biosensing

Genipin is a naturally occurring nontoxic cross-linker, which has been widely used for drug delivery due to its excellent biocompatibility, admirable biodegradability and stable cross-linked attributes. These advantages led to its extensive application in the fabrication of hydrogels for drug delivery. This review describes the physicochemical characteristics and pharmacological activities of genipin and attempts to elucidate the detailed mechanisms of the cross-linking reaction between genipin and biomaterials. The current article entails a general review of the different biomaterials cross-linked by genipin: chitosan and its derivatives, collagen, gelatin, etc. The genipin-cross-linked hydrogels for various pharmaceutical applications, including ocular drug delivery, buccal drug delivery, oral drug delivery, anti-inflammatory drug delivery, and antibiotic and antifungal drug delivery, are reported. Finally, the future research directions and challenges of genipin-cross-linked hydrogels for pharmaceutical applications are also discussed in this review.

Genipin-cross-linked hydrogels based on biomaterials for drug delivery: a review.

Comparative studies on ZIF-8 and SiO₂ nanoparticles as carrier for immobilized β-glucosidase

Immobilization of β-glucosidase by self-catalysis and compared to crosslinking with glutaraldehyde.

The effects of NaCl on enzyme encapsulation by zeolitic imidazolate frameworks-8.

(S)-Mandelate dehydrogenase (SMDH) and laccase were immobilized on chitosan. The bi-enzymatic system with immobilized SMDH and immobilized laccase was taken to catalyze the stereoselective transformation of racemic mandelic acid and (R)-mandelic acid was obtained from its racemic mixture. Characteristics of the immobilized enzymes were valuated. The optimum pH and temperature of the immobilized SMDH were found to be pH 3.4 and 45 °C, and these of the immobilized laccase were about pH 6.0 and 55 °C, respectively. The K
 m value of the immobilized SMDH for racemic mandelic acid was 0.27 mM and that of the immobilized laccase for ferrocyanide was 0.99 mM. The thermal and storage stabilities of these enzymes were improved with immobilization. The enantiomeric purity of the bi-enzymatically produced (R)-mandelic acid was determined to be over 99%. The immobilized bi-enzymatic system for the stereoselective transformation of racemic mandelic acid showed higher productivity, faster reaction velocity, and more stable catalytic ability.

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Xuan Zhang

Papers

Comparative studies on ZIF-8 and SiO₂ nanoparticles as carrier for immobilized β-glucosidase

Immobilization of β-glucosidase by self-catalysis and compared to crosslinking with glutaraldehyde.

The effects of NaCl on enzyme encapsulation by zeolitic imidazolate frameworks-8.

Stereoselective biotransformation of racemic mandelic acid using immobilized laccase and (S)-mandelate dehydrogenase.

A convenient and rapid method for detecting d-glucose in honey used smartphone