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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pawlik, Anna Wójcik, Magdalena Rulka, Karol Motyl-Gorzel, Karolina Osinska-Jaroszuk, Monika Wielbo, Jerzy Marek-Kozaczuk, Monika Skorupska, Anna Rogalski, Jerzy Janusz, Grzegorz |
| Description | Author Affiliation: Pawlik A ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland. Electronic address: anna.pawlik@poczta.umcs.lublin.pl.); Wójcik M ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland); Rulka K ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Motyl-Gorzel K ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Osinska-Jaroszuk M ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Wielbo J ( Department of Genetics and Microbiology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Marek-Kozaczuk M ( Department of Genetics and Microbiology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Skorupska A ( Department of Genetics and Microbiology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Rogalski J ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.); Janusz G ( Department of Biochemistry, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland.) |
| Abstract | The soil native bacterial strains were screened for laccase activity. Bacterial strain L3.8 with high laccase activity was identified as Sinorhizobium meliloti. The crude intracellular L3.8 enzyme extract was able to oxidize typical diagnostic substrates of plant and fungal laccases. Laccase L3.8 was purified 81-fold with a yield of 19.5%. The molecular mass of the purified bacterial laccase was found to be 70.0kDa and its pI was 4.77. UV-vis spectrum showed that L3.8 protein is a multicopper oxidase. The carbohydrate content of the purified enzyme was estimated at 3.2%. Moreover, the laccase active fraction was characterized in terms of kinetics, temperature, and pH optima as well as the effect of various chemical compounds on the laccase activity, and antioxidant properties, which indicated that the L3.8 laccase had unique properties that might be important in biotechnological applications. The lacc gene encoding S. meliloti laccase was cloned and characterized. The full-length sequence of 1950bp encoded a protein of 649 aa preceded by a signal peptide consisting of 26aa. Laccase L3.8 shared significant structural features characteristic of other laccases, including the conserved regions of four histidine-rich copper-binding sites. Potential biotechnological importance of a newly identified laccase is discussed. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 92 |
| e-ISSN | 18790003 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-11-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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