Irina I. Romanovska
A.V. Bogatsky Physico-Chemical Institute of the National Academy of Sciences of Ukraine, Odesa, Ukraine
Oleksandra A. Rizhak
A.V. Bogatsky Physico-Chemical Institute of the National Academy of Sciences of Ukraine, Odesa, Ukraine
Svetlana S. Dekina
A.V. Bogatsky Physico-Chemical Institute of the National Academy of Sciences of Ukraine, Odesa, Ukraine
Yuliia A. Shesterenko
A.V. Bogatsky Physico-Chemical Institute of the National Academy of Sciences of Ukraine, Odesa, Ukraine
Yevgeniia A. Shesterenko
A.V. Bogatsky Physico-Chemical Institute of the National Academy of Sciences of Ukraine, Odesa, Ukraine
Pagination: 188-198
DOI: https://doi.org/10.15407/akademperiodyka.444.188
REFERENCES
- Gurung N., Ray S., Bose S., Rai V. A broader view: Microbial enzymes and their relevance in industries, medicine, and beyond. BioMed. Res. Int. 2013. 13: 1–18. https://doi.org/10.1155/2013/329121
- Sivaramakrishnan G., Sridharan K.J. Role of serratiopeptidase after surgical removal of smpacted molar: A systematic review and meta-analysis. Maxillofacial and Oral Surgery. 2018. 17(2): 122–128. https://doi.org/10.1007/s12663-017-0996-9
- Jadav S.P., Patel N.H., Shah T.G., Gajera M.V., Trivedi H.R., Shah B.K. Comparison of anti-inflammatory activity of serratiopeptidase and diclofenac in albino rats. J. Pharmacol. Pharmacother. 2010. 1(2): 116–117. https://doi.org/10.4103/0976-500X.72362
- Singh R., Mittal A., Kumar M., Mehta P. Microbial protease in commercial applications. J. Pharm. Chem. Biol. Sci. 2016. 4(3): 365–374.
- Maheshwari M., Miglani G., Mali A., Paradkar A., Yamamura S., Kadam S. Development of tetracycline-serratiopeptidase-containing periodontal gel: formulation and preliminary clinical study. AAPS Pharm. Sci. Tech. 2006. 7(3): E162–E171. https://doi.org/10.1208/pt070376
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 1969. 244: 4406–4412. https://doi.org/10.1016/S0021-9258(18)94333-4
- Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 1970. 227(5259): 680–685. https://doi.org/10.1038/227680a0
- Bonner P.L.R., Hargreaves A.J. Basic bioscience laboratory techniques: a pocket guide. John Wiley Sons. 2011. 232 p.
- Hartree E.F. Determination of protein: а modification of the Lowry method that gives a linear photometric response. Anal. Biochemistry. 1972. 48(2): 422–427. https://doi.org/10.1016/0003-2697(72)90094-2
- Petrova I.S., Vintsyunaite M.M. Determination of proteolytic activity of enzyme preparations of microbial origin. Prikladnaya biokhimiya i mikrobiologiya. 1966. 2(3): 322–327. (in Russian).
- Masada M. Determination of the thrombolytic activity of Natto extract. Food Style. 2004. 8(1): 92–95.
- Yokoyama S., Hiramatsu J.-I. A modified ninhydrin reagent using ascorbic acid instead of potassium cyanide. J. Bioscience Bioengineering. 2003. 95(2): 204–205. https://doi.org/10.1016/S1389-1723(03)80131-7
- Dekina S.S., Romanovska I.I., Leonenko І.І., Yegorova A.V. Mucoadhesive gel with immobilized lysozyme: preparation and properties. Biotechnologia Acta. 2015. 8(3): 104–109. https://doi.org/10.15407/biotech8.03.104
- Tager A.A. Physicochemistry of polymers (Fizikokhimiya polimerov). Moscow, 2007. 536 p. (in Russian).
- Keleti T. Fundamentals of Enzymatic Kinetics (Osnovy fermentativnoy kinetiki). Moscow: Mir, 1990. 348 p. (in Russian).
- Hamada K., Hata Y., Katsuya Y., Hiramatsu H., Fujiwara T., Katsube Y. Crystal structureof Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0 Å resolution. J. Biochem. 1996. 119(5): 844–851. https://doi.org/10.1093/oxfordjournals.jbchem.a021320
- Vos P., Faas M.M., Strand B., Calafiore R. Alginate-based microcapsules for immunoisolation of pancreatic islets. Biomaterials. 2006. 27(32): 5603–5617. https://doi.org/10.1016/j.biomaterials.2006.07.010
- Kamoun E.A., Kenawy E.S., Tamer T.M. et al. Poly(vinyl alcohol)-alginate physically crosslinked hydrogel membranes for wound dressing applications: Characterization and bio-evaluation. Arabian J. Chem. 2015. 8(1): 38–47. https://doi.org/10.1016/j.arabjc.2013.12.003
- Illum L., Casettari L. Chitosan in nasal delivery systems for therapeutic drugs. J. Controlled Release. 2014. 190: 189–200. https://doi.org/10.1016/j.jconrel.2014.05.003
- Thomas C., Keleher J., Kevin J., Bianca G. et al. Synthesis and characterization of a chitosan/PVA antimicrobial hydrogel nanocomposite for responsive wound management materials. J. Microb. Biochem. Tech. 2016. 8(2): 65–70. https://doi.org/10.4172/1948-5948.1000264
- Dekina S., Romanovska I., Sevastyanov O., Shesterenko Ye., Ryjak A., Varbanets L., Dzubluk N., Muratov E. Development and Characterization of Chitosan/Polyvinyl Alcohol Polymer Material with Elastolytic and Collagenolytic Activities. Enzyme Microbial Technology. 2020. 132: 1093–1099. https://doi.org/10.1016/j.enzmictec.2019.109399
- Liu Y., Chen J.Y. Enzyme immobilization on cellulose matrixes. J. Bioactive Compatible Polymers. 2016. 31(6): 553–567. https://doi.org/10.1177/0883911516637377
- Wui T., Nor W., Ramli A. Carboxymethylcellulose film for bacterial wound infection control and healing. Carbohydr. Polym. 2014. 112: 367–375. https://doi.org/10.1016/j.carbpol.2014.06.002
- Basu P., Narendrakumar U., Arunachalam R., Dev S. Characterization and Evaluation of Carboxymethyl Cellulose-Based Films for Healing of Full-Thickness Wounds in Normal and Diabetic Rats. ACS Omega. 2018. 3(10): 12622−12632. https://doi.org/10.1021/acsomega.8b02015
- Romanovska I.I., Dekina S.S., Ryzhak O.A., Sevastyanov O.V., Shesterenko E.A., Shesterenko Yu.A. Properties of proteolytic enzyme serrathiopeptidase and search for biocompatible matrices for immobilization. In: New functional substances and materials of chemical production. Kyiv, 2019. P. 40–41. (in Ukrainian).
- Raza F., Zafar H., Zhu Y., Ren Y. A review on recent advances in stabilizing peptides/proteins upon fabrication in hydrogels from biodegradable polymers. Pharmaceutics. 2018. 10(1): 16–21. https://doi.org/10.3390/pharmaceutics10010016
- Mashkovsky M.D. Medicines (Lekarstvennyye sredstva). Moscow, 2012, 1216 p. (in Russian).
- Patent of Ukrainian No. 121937. Romanovska I.I., Ryzhak O.A., Sevastyanov O.V. et al. Wound healing bandage with proteolytic activity. Publ. 10.08.2020.
- Nwagu T.N., Ugwuodo C.J. Stabilizing bromelain for therapeutic applications by adsorption immobilization on spores of probiotic Bacillus. Int. J. Biol. Macromol. 2019. 127: 406–414. https://doi.org/10.1016/j.ijbiomac.2019.01.061
- Thakrar F.J., Singh S.P. Catalytic, thermodynamic and structural properties of an immobilized and highly thermostable alkaline protease from a haloalkaliphilic actinobacteria, Nocardiopsis alba TATA-5. Bioresour. Technol. 2019. 278: 150–158. https://doi.org/10.1016/j.biortech.2019.01.058