Articolo in rivista, 2018, ENG, 10.1166/jnn.2018.14333

Soluble and Nanoporous Silica Gel-Entrapped C-freundii Methionine gamma-Lyase

Morozova EA, Kulikova VV, Faggiano S, Raboni S, Gabellieri E, Cioni P, Anufrieva NV, Revtovich SV, Demidkina T, Mozzarelli A

Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 119991, Russia Univ Parma, Dept Food & Drug, I-43124 Parma, Italy CNR, Inst Biophys, I-56124 Pisa, Italy

Methionine gamma-lyase is a pyridoxal 5'-phosphate dependent tetramer that catalyzes the alpha, gamma-elimination of methionine in ammonia, methanethiol and alpha-ketobutyrate. MGL catalytic power has been exploited as a therapeutic strategy to reduce the viability of cancer cells or bacteria. In order to obtain a stable enzyme to be delivered at the site of action, MGL can be encapsulated in a variety of matrices. As a reference encapsulation strategy we have prepared MGL nanoporous wet silica gels. Immobilized MGL gels were characterized with regards to activity, stability, absorption, circular dichroism and fluorescence properties and compared with soluble MGL. We found that MGL gels exhibit (i) spectroscopic properties very similar to MGL in solution, (ii) a higher stability with respect to the soluble enzyme and (iii) catalytic activity six-fold lower than in solution. These findings prove that MGL encapsulation is a suitable strategy for therapeutic applications.

Journal of nanoscience and nanotechnology (Print) 18 (3), pp. 2210–2219

Keywords

Methionine; Protein Drug; Protein Encapsulation; Pyridoxal Phosphate; Enzyme Activity; Fluorescence

CNR authors

Mozzarelli Andrea, Raboni Samanta, Gabellieri Edi, Cioni Patrizia

CNR institutes

IBF – Istituto di biofisica

ID: 387270

Year: 2018

Type: Articolo in rivista

Creation: 2018-05-15 13:11:15.000

Last update: 2021-04-08 17:11:36.000

External IDs

CNR OAI-PMH: oai:it.cnr:prodotti:387270

DOI: 10.1166/jnn.2018.14333

ISI Web of Science (WOS): 000426033400124