TY  - JOUR
AU  - Miladinov, Nataša
AU  - Kojić, Milan
AU  - Arsenijević, Slavica
AU  - Lozo, Jelena
AU  - Topisirović, Ljubiša
PY  - 2001
UR  - http://intor.torlakinstitut.com/handle/123456789/796
AB  - Soj Lactococcus lactis subsp. lactis BGIS29 je prirodni izolat iz sira proizvedenog u domaćinstvu koji proizvodi bakteriocin IS29 i proteinazu PI-tipa. Rezultati dobijeni biohemijskom karakterizacijom bakteriocina IS29 sugerišu da on pripada klasi II bakteriocina. DNK-DNK hibridizacija i PFGE analiza su pokazali da su geni za proteinazu i proizvodnju bakteriocina locirani na različitim genetičkim elem- entima. Proizvodila proteinaze coja BGIS29 i bakteriocina IS29 zavise od koncentracije kazitona u medijumu za rast bakterija. Veće koncentracije kazitona imaju inhibitorni efekat na aktivnost proteinaze. Nasuprot tome, proizvodila bakteriocina IS29 je izraženija u medijumu koji sadrži veće koncentracije kazitona.
AB  - Strain Lactacoccus lactis subsp. lactis BGIS29, a natural isolate from homemade cheese produces the bacteriocin IS29 and the Pi-type proteinase. The results obtained by biochemical characterization of bacteriocin IS29 suggest that it belongs to class II of bacteriocins. The DNA-DNA hybridization and PFGE analysis showed that the genes for proteinase and bacteriocin production are located on separate genetic elements. Production of the proteinase of BGIS29 and the bacteriocin IS29 depend on the concentration of casitone in medium. Higher concentrations of casitone expressed an inhibitory effect on the proteinase activity. In contrast, production of bacteriocin IS29 was more pronounced in medium containing high casitone concentrations.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Karakterizacija prirodnog izolata Lactococcus lactis subsp. lactis BGIS29, proizvođača bakteriocina IS29 i proteinaze vezane za ćelijski zid
T1  - Characterisation of natural isolate Lactococcus lactis subsp. lactis BGIS29, a strain producing bacteriocin IS29 and cell wall-associated proteinase
EP  - 16
IS  - 1-2
SP  - 7
VL  - 53
UR  - https://hdl.handle.net/21.15107/rcub_intor_796
ER  - 

@article{
author = "Miladinov, Nataša and Kojić, Milan and Arsenijević, Slavica and Lozo, Jelena and Topisirović, Ljubiša",
year = "2001",
abstract = "Soj Lactococcus lactis subsp. lactis BGIS29 je prirodni izolat iz sira proizvedenog u domaćinstvu koji proizvodi bakteriocin IS29 i proteinazu PI-tipa. Rezultati dobijeni biohemijskom karakterizacijom bakteriocina IS29 sugerišu da on pripada klasi II bakteriocina. DNK-DNK hibridizacija i PFGE analiza su pokazali da su geni za proteinazu i proizvodnju bakteriocina locirani na različitim genetičkim elem- entima. Proizvodila proteinaze coja BGIS29 i bakteriocina IS29 zavise od koncentracije kazitona u medijumu za rast bakterija. Veće koncentracije kazitona imaju inhibitorni efekat na aktivnost proteinaze. Nasuprot tome, proizvodila bakteriocina IS29 je izraženija u medijumu koji sadrži veće koncentracije kazitona., Strain Lactacoccus lactis subsp. lactis BGIS29, a natural isolate from homemade cheese produces the bacteriocin IS29 and the Pi-type proteinase. The results obtained by biochemical characterization of bacteriocin IS29 suggest that it belongs to class II of bacteriocins. The DNA-DNA hybridization and PFGE analysis showed that the genes for proteinase and bacteriocin production are located on separate genetic elements. Production of the proteinase of BGIS29 and the bacteriocin IS29 depend on the concentration of casitone in medium. Higher concentrations of casitone expressed an inhibitory effect on the proteinase activity. In contrast, production of bacteriocin IS29 was more pronounced in medium containing high casitone concentrations.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Karakterizacija prirodnog izolata Lactococcus lactis subsp. lactis BGIS29, proizvođača bakteriocina IS29 i proteinaze vezane za ćelijski zid, Characterisation of natural isolate Lactococcus lactis subsp. lactis BGIS29, a strain producing bacteriocin IS29 and cell wall-associated proteinase",
pages = "16-7",
number = "1-2",
volume = "53",
url = "https://hdl.handle.net/21.15107/rcub_intor_796"
}

Miladinov, N., Kojić, M., Arsenijević, S., Lozo, J.,& Topisirović, L.. (2001). Karakterizacija prirodnog izolata Lactococcus lactis subsp. lactis BGIS29, proizvođača bakteriocina IS29 i proteinaze vezane za ćelijski zid. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 53(1-2), 7-16.
https://hdl.handle.net/21.15107/rcub_intor_796

Miladinov N, Kojić M, Arsenijević S, Lozo J, Topisirović L. Karakterizacija prirodnog izolata Lactococcus lactis subsp. lactis BGIS29, proizvođača bakteriocina IS29 i proteinaze vezane za ćelijski zid. in Archives of Biological Sciences. 2001;53(1-2):7-16.
https://hdl.handle.net/21.15107/rcub_intor_796 .

Miladinov, Nataša, Kojić, Milan, Arsenijević, Slavica, Lozo, Jelena, Topisirović, Ljubiša, "Karakterizacija prirodnog izolata Lactococcus lactis subsp. lactis BGIS29, proizvođača bakteriocina IS29 i proteinaze vezane za ćelijski zid" in Archives of Biological Sciences, 53, no. 1-2 (2001):7-16,
https://hdl.handle.net/21.15107/rcub_intor_796 .

TY  - JOUR
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
AU  - Fira, Đorđe
AU  - Miladinov, Nataša
AU  - Strahinić, Ivana
AU  - Gajić, Olivera
AU  - Arsenijević, Slavica
AU  - Spasojević, Irena
AU  - Vukasinović, Maja
PY  - 2000
UR  - http://intor.torlakinstitut.com/handle/123456789/793
AB  - Autohtoni sojevi bakterija mlečne kiseline (BMK) su izolovane iz fermentisanih mlečnih proizvoda rađenih u domaćoj radinosti. Fermentisani mlečni proizvodi su sakupljani sa specifičnih ekoloških lokaliteta kao što su visoke planine (iznad 1200 m nadmorske visine), planinske visoravni, rečne doline, ostrva, obala Jadranskog mora, itd. Analiza kolekcije prirodnih izolata BMK je pokazala da izolati proizvode proteinaze, bakteriocine i egzopolisaharide. Pokazano je, takođe, da neki izolati laktokoka i laktobacila proizvode istovremeno dva različita bakteriocina. Pored toga određeni broj izolata proizvodi i proteinaze i bakteriocine. Nađeno je da prirodni izolati sintetišu specifične proteinaze. Analiza organizacije prt gena u prirodnim izolatima BMK je pokazala da četiri laktobacila poseduju organizaciju prt gena koja se razlikuje od do sada opisanih. Izučavanje regulacije gena koji kodiraju proteinaze, bakteriocine ili egzopolisaharide može olakšati konstrukciju specifičnih starter kultura za proizvodnju autohtonih fermentisanih mlečnih proizvoda, tj. fermentisanih proizvoda sa geografskim poreklom.
AB  - Autochthonous strains of lactic acid bacteria (LAB) were isolated from homemade fermented milk products. These products were collected from specific ecological localities such as high mountains (above 1200 m above sea level) mountain plateaus, river valleys, islands, Adriatic coast, etc. Analysis of LAB from the collection of natural isolates revealed that they produce proteinases, bacteriocins and exopolysaccharides. It was also shown that some isolates of lactococci and lactobacilli produce two bacteriocins simultaneously. According to their antimicrobial and biochemical properties most of the analyzed bacteriocins in natural isolates of lactococci were class 11 bacteriocins. In addition some isolates produced both proteinase and bacteriocin. Biosynthesis of specific proteinases was detected in natural isolates. Analysis of the prt gene organization among natural isolates of LAB showed that four isolates of lactobacilli exhibited prt genes organization different from those described so far. Elucidation of the regulation of the genes encoding proteinases, bacteriocins and exopolysaccharides could facilitate the construction of specific starter cultures for production of autochthonous fermented milk products, i.e. fermented products with a geographical origin.
PB  - Društvo genetičara Srbije, Beograd
T2  - Genetika-Belgrade
T1  - Molekularna genetika autohtonih bakterija mlečne kiseline
T1  - Molecular genetics of autochthonous lactic acid bacteria
EP  - 127
IS  - 2
SP  - 115
VL  - 32
UR  - https://hdl.handle.net/21.15107/rcub_intor_793
ER  - 

@article{
author = "Topisirović, Ljubiša and Kojić, Milan and Fira, Đorđe and Miladinov, Nataša and Strahinić, Ivana and Gajić, Olivera and Arsenijević, Slavica and Spasojević, Irena and Vukasinović, Maja",
year = "2000",
abstract = "Autohtoni sojevi bakterija mlečne kiseline (BMK) su izolovane iz fermentisanih mlečnih proizvoda rađenih u domaćoj radinosti. Fermentisani mlečni proizvodi su sakupljani sa specifičnih ekoloških lokaliteta kao što su visoke planine (iznad 1200 m nadmorske visine), planinske visoravni, rečne doline, ostrva, obala Jadranskog mora, itd. Analiza kolekcije prirodnih izolata BMK je pokazala da izolati proizvode proteinaze, bakteriocine i egzopolisaharide. Pokazano je, takođe, da neki izolati laktokoka i laktobacila proizvode istovremeno dva različita bakteriocina. Pored toga određeni broj izolata proizvodi i proteinaze i bakteriocine. Nađeno je da prirodni izolati sintetišu specifične proteinaze. Analiza organizacije prt gena u prirodnim izolatima BMK je pokazala da četiri laktobacila poseduju organizaciju prt gena koja se razlikuje od do sada opisanih. Izučavanje regulacije gena koji kodiraju proteinaze, bakteriocine ili egzopolisaharide može olakšati konstrukciju specifičnih starter kultura za proizvodnju autohtonih fermentisanih mlečnih proizvoda, tj. fermentisanih proizvoda sa geografskim poreklom., Autochthonous strains of lactic acid bacteria (LAB) were isolated from homemade fermented milk products. These products were collected from specific ecological localities such as high mountains (above 1200 m above sea level) mountain plateaus, river valleys, islands, Adriatic coast, etc. Analysis of LAB from the collection of natural isolates revealed that they produce proteinases, bacteriocins and exopolysaccharides. It was also shown that some isolates of lactococci and lactobacilli produce two bacteriocins simultaneously. According to their antimicrobial and biochemical properties most of the analyzed bacteriocins in natural isolates of lactococci were class 11 bacteriocins. In addition some isolates produced both proteinase and bacteriocin. Biosynthesis of specific proteinases was detected in natural isolates. Analysis of the prt gene organization among natural isolates of LAB showed that four isolates of lactobacilli exhibited prt genes organization different from those described so far. Elucidation of the regulation of the genes encoding proteinases, bacteriocins and exopolysaccharides could facilitate the construction of specific starter cultures for production of autochthonous fermented milk products, i.e. fermented products with a geographical origin.",
publisher = "Društvo genetičara Srbije, Beograd",
journal = "Genetika-Belgrade",
title = "Molekularna genetika autohtonih bakterija mlečne kiseline, Molecular genetics of autochthonous lactic acid bacteria",
pages = "127-115",
number = "2",
volume = "32",
url = "https://hdl.handle.net/21.15107/rcub_intor_793"
}

Topisirović, L., Kojić, M., Fira, Đ., Miladinov, N., Strahinić, I., Gajić, O., Arsenijević, S., Spasojević, I.,& Vukasinović, M.. (2000). Molekularna genetika autohtonih bakterija mlečne kiseline. in Genetika-Belgrade
Društvo genetičara Srbije, Beograd., 32(2), 115-127.
https://hdl.handle.net/21.15107/rcub_intor_793

Topisirović L, Kojić M, Fira Đ, Miladinov N, Strahinić I, Gajić O, Arsenijević S, Spasojević I, Vukasinović M. Molekularna genetika autohtonih bakterija mlečne kiseline. in Genetika-Belgrade. 2000;32(2):115-127.
https://hdl.handle.net/21.15107/rcub_intor_793 .

Topisirović, Ljubiša, Kojić, Milan, Fira, Đorđe, Miladinov, Nataša, Strahinić, Ivana, Gajić, Olivera, Arsenijević, Slavica, Spasojević, Irena, Vukasinović, Maja, "Molekularna genetika autohtonih bakterija mlečne kiseline" in Genetika-Belgrade, 32, no. 2 (2000):115-127,
https://hdl.handle.net/21.15107/rcub_intor_793 .

TY  - JOUR
AU  - Fira, Đorđe
AU  - Kojić, Milan
AU  - Strahinić, Ivana
AU  - Arsenijević, Slavica
AU  - Banina, Ana
AU  - Topisirović, Ljubiša
PY  - 2000
UR  - http://intor.torlakinstitut.com/handle/123456789/792
AB  - Enterococcus faecalis BGPM3 proizvodi proteinazu sposobnu da hidrolizuje ukupan kazein kao i frakcije αs1-, β-, i k-kazeina. Ova proteinaza, takođe, hidrolizuje želatin, ali ne deluje na denaturisani goveđi serum albumin ili hemoglobin. Ustanovljeno je da se optimalna hidroliza kazeina u prisuetvu BGPM3 proteinaze postiže na pH 6.5, a njegova maksimalna hidroliza na 37°C. Prisustvo proteolitičke aktivnosti u supernatantu, koji ne sadrži žive ćelije, ukazuje da izolat E. faecalis BGPM3 proizvodi ekstracelularnu proteinazu. Sinteza ove proteinaze se odigrava tokom celokupnog ciklusa rasta bakterije, pri čemu se maksimum proizvodnje postiže u stacionarnoj fazi. Trstman BGPM3 proteinaze sa helatorima metalnih jona dovodi do potpunog gubitka proteolitičke aktivnosti. Međutim, moguće je povratiti proteolitičku aktivnost (do 75%) ako se tretiranom enzimu dodaju joni Zn2+ što ukazuje da je BGPM3 proteinaza metaloenzim. Proteolitička aktivnost ovog enzima je inhibirana jonima Cu2+, čak i u prisustvu jona Zn2+. Eksperimentalni rezultati ukazuju da je proizvodnja BGPM3 proteinaze indudibilna, tj., dolazi do povećanja njene sinteze kada bakterija raste u prisustvu smeše oligopeptida (kazitona). Tako se dobija desetostruko povećanje proteolitičke aktivnosti u bezćelijskom supernatantu kada se pripremi iz kulture koja sadrži kaziton. Određivanje molekulske mase BGPM3 proteinaze je pokazalo da je to protein od oko 29 kDa.
AB  - Enterococcus faecalis BGPM3 produces a proteinase that hydrolyzes total casein as well as α s1-, β-, and k-casein fractions. This proteinase was also able to hydrolyse gelatine, but not denatured bovine serum albumin and haemoglobin. The optimal pH of casein hydrolysis was 6.5 (determined at 30°C). Maximum caseinolytic activity was obtained at 37°C. The presence of proteolytic activity in cell-free supernatant strongly indicated that E. faecalis BGPM3 produces strictly extracellular proteinase. Proteinase production occurred through the growth cycle reaching a maximum at stationary phase. Pretreatment of the BGPM3 proteinase with metal ion chelators resulted in a total loss of proteolytic activity. Restoration of activity (75%) was obtained only with Zn2+ suggesting that the BGPM3 proteinase is zinc-metalloenzyme. Cu2+ even in the presence of Zn2+ inhibited proteolytic activity. It seems that production of proteinase is induced by oligopeptides (casitone), since 10-fold higher proteolytic activity was obtained in the cell-free supernatant prepared from the cultures containing casitone. The molecular mass determination revealed that extracellular BGPM3 proteinase has a molecular mass of about 29 kDa.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Proizvodnja inducibilne ekstracelularne proteinaze pomoću prirodnog izolata Enterococcus faecalis BGPM3
T1  - Natural isolate Enterococcus faecalis BGPM3 produces an inducible extracellular proteinase
EP  - 76
IS  - 2
SP  - 67
VL  - 52
UR  - https://hdl.handle.net/21.15107/rcub_intor_792
ER  - 

@article{
author = "Fira, Đorđe and Kojić, Milan and Strahinić, Ivana and Arsenijević, Slavica and Banina, Ana and Topisirović, Ljubiša",
year = "2000",
abstract = "Enterococcus faecalis BGPM3 proizvodi proteinazu sposobnu da hidrolizuje ukupan kazein kao i frakcije αs1-, β-, i k-kazeina. Ova proteinaza, takođe, hidrolizuje želatin, ali ne deluje na denaturisani goveđi serum albumin ili hemoglobin. Ustanovljeno je da se optimalna hidroliza kazeina u prisuetvu BGPM3 proteinaze postiže na pH 6.5, a njegova maksimalna hidroliza na 37°C. Prisustvo proteolitičke aktivnosti u supernatantu, koji ne sadrži žive ćelije, ukazuje da izolat E. faecalis BGPM3 proizvodi ekstracelularnu proteinazu. Sinteza ove proteinaze se odigrava tokom celokupnog ciklusa rasta bakterije, pri čemu se maksimum proizvodnje postiže u stacionarnoj fazi. Trstman BGPM3 proteinaze sa helatorima metalnih jona dovodi do potpunog gubitka proteolitičke aktivnosti. Međutim, moguće je povratiti proteolitičku aktivnost (do 75%) ako se tretiranom enzimu dodaju joni Zn2+ što ukazuje da je BGPM3 proteinaza metaloenzim. Proteolitička aktivnost ovog enzima je inhibirana jonima Cu2+, čak i u prisustvu jona Zn2+. Eksperimentalni rezultati ukazuju da je proizvodnja BGPM3 proteinaze indudibilna, tj., dolazi do povećanja njene sinteze kada bakterija raste u prisustvu smeše oligopeptida (kazitona). Tako se dobija desetostruko povećanje proteolitičke aktivnosti u bezćelijskom supernatantu kada se pripremi iz kulture koja sadrži kaziton. Određivanje molekulske mase BGPM3 proteinaze je pokazalo da je to protein od oko 29 kDa., Enterococcus faecalis BGPM3 produces a proteinase that hydrolyzes total casein as well as α s1-, β-, and k-casein fractions. This proteinase was also able to hydrolyse gelatine, but not denatured bovine serum albumin and haemoglobin. The optimal pH of casein hydrolysis was 6.5 (determined at 30°C). Maximum caseinolytic activity was obtained at 37°C. The presence of proteolytic activity in cell-free supernatant strongly indicated that E. faecalis BGPM3 produces strictly extracellular proteinase. Proteinase production occurred through the growth cycle reaching a maximum at stationary phase. Pretreatment of the BGPM3 proteinase with metal ion chelators resulted in a total loss of proteolytic activity. Restoration of activity (75%) was obtained only with Zn2+ suggesting that the BGPM3 proteinase is zinc-metalloenzyme. Cu2+ even in the presence of Zn2+ inhibited proteolytic activity. It seems that production of proteinase is induced by oligopeptides (casitone), since 10-fold higher proteolytic activity was obtained in the cell-free supernatant prepared from the cultures containing casitone. The molecular mass determination revealed that extracellular BGPM3 proteinase has a molecular mass of about 29 kDa.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Proizvodnja inducibilne ekstracelularne proteinaze pomoću prirodnog izolata Enterococcus faecalis BGPM3, Natural isolate Enterococcus faecalis BGPM3 produces an inducible extracellular proteinase",
pages = "76-67",
number = "2",
volume = "52",
url = "https://hdl.handle.net/21.15107/rcub_intor_792"
}

Fira, Đ., Kojić, M., Strahinić, I., Arsenijević, S., Banina, A.,& Topisirović, L.. (2000). Proizvodnja inducibilne ekstracelularne proteinaze pomoću prirodnog izolata Enterococcus faecalis BGPM3. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 52(2), 67-76.
https://hdl.handle.net/21.15107/rcub_intor_792

Fira Đ, Kojić M, Strahinić I, Arsenijević S, Banina A, Topisirović L. Proizvodnja inducibilne ekstracelularne proteinaze pomoću prirodnog izolata Enterococcus faecalis BGPM3. in Archives of Biological Sciences. 2000;52(2):67-76.
https://hdl.handle.net/21.15107/rcub_intor_792 .

Fira, Đorđe, Kojić, Milan, Strahinić, Ivana, Arsenijević, Slavica, Banina, Ana, Topisirović, Ljubiša, "Proizvodnja inducibilne ekstracelularne proteinaze pomoću prirodnog izolata Enterococcus faecalis BGPM3" in Archives of Biological Sciences, 52, no. 2 (2000):67-76,
https://hdl.handle.net/21.15107/rcub_intor_792 .