Segmented Polyurethanes for Medical Applications: Synthesis, Characterization andin vitro Enzymatic Degradation Studies

2001 ◽  
Vol 169 (1) ◽  
pp. 261-272 ◽  
Author(s):  
Gianluca Ciardelli ◽  
Alfonsina Rechichi ◽  
Piero Cerrai ◽  
Mario Tricoli ◽  
Niccoletta Barbani ◽  
...  
2018 ◽  
Vol 155 ◽  
pp. 84-94 ◽  
Author(s):  
Carmen Valverde ◽  
Gerard Lligadas ◽  
Juan C. Ronda ◽  
Marina Galià ◽  
Virginia Cádiz

2010 ◽  
Vol 6 (6) ◽  
pp. 2035-2044 ◽  
Author(s):  
L.H. Chan-Chan ◽  
R. Solis-Correa ◽  
R.F. Vargas-Coronado ◽  
J.M. Cervantes-Uc ◽  
J.V. Cauich-Rodríguez ◽  
...  

2017 ◽  
Vol 74 (12) ◽  
pp. 5181-5194
Author(s):  
Juntima Pradid ◽  
Wirunya Keawwatana ◽  
Upsorn Boonyang ◽  
Siree Tangbunsuk

Biomaterials ◽  
1997 ◽  
Vol 18 (21) ◽  
pp. 1411-1415 ◽  
Author(s):  
Giovanni Abatangelo ◽  
Rolando Barbucci ◽  
Paola Brun ◽  
Stefania Lamponi

2019 ◽  
Author(s):  
Sandeep Kaur Saggu ◽  
Gopaljee Jha ◽  
Prakash Chandra Mishra

AbstractEnzymes have replaced or decreased usage of toxic chemicals for industrial and medical applications leading towards sustainable chemistry. In this study, we report purification and characterization of a biofilm degrading protease secreted by Microbacterium sp. SKS10. The protease was identified as a metalloprotease, Peptidase M16 using mass spectrometry. It showed optimum activity at 60 °C, pH 12 and retained its activity in the presence of various salts and organic solvents. The enzyme was able to degrade biofilms efficiently at enzyme concentration lower than other known enzymes such as papain, trypsin and □-amylase. The presence of this protease increased the accessibility of antibiotics inside the biofilm, and was found to be non-cytotoxic towards human epidermoid carcinoma cells (A431) at the effective concentration for biofilm degradation. Thus, this protease may serve as an effective tool for management of biofilms.


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