Characterization of cell envelope-associated proteinases of thermophilic lactobacilli
Само за регистроване кориснике
2001
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The proteolytic activities of two natural isolates of thermophilic lactobacilli, Lactobacillus acidophilus BGRA43 and Lact, delbrueckii BGPF1, and Lact. acidophilus CH2 (Chr. Hansen's strain) and Lact, acidophilus V74 (Visby's strain), were compared. Results revealed that optimal pH for all four proteinases is 6.5, whereas temperature optimum varied among proteinases. Determination of caseinolytic activity done under optimal conditions for each strain revealed that the CH2 and V74 proteinases completely hydrolysed both alpha (s1)-casein and beta -casein, showing very low activity towards kappa -casein. The BGPF1 proteinase completely hydrolysed only beta -casein. The BGRA43 proteinase completely hydrolysed all three casein fractions. The proteolytic activities of whole cells were inhibited by serine proteinase inhibitors, suggesting that all four strains produce serine proteinases. DNA-DNA hybridization and PCR analysis showed that BGPF1 contains the prtB-like proteinase gene. Characte...rized thermophilic strains BGPF1 and BGRA43 were successfully used as starter cultures for production of yoghurt and acidophilus milk, respectively.
Извор:
Journal of Applied Microbiology, 2001, 90, 1, 123-130Издавач:
- Wiley
DOI: 10.1046/j.1365-2672.2001.01226.x
ISSN: 1364-5072
PubMed: 11155131
WoS: 000167055000014
Scopus: 2-s2.0-0035122197
Институција/група
TorlakTY - JOUR AU - Fira, Đorđe AU - Kojić, Milan AU - Banina, Ana AU - Spasojević, I AU - Strahinić, Ivana AU - Topisirović, Ljubiša PY - 2001 UR - http://intor.torlakinstitut.com/handle/123456789/715 AB - The proteolytic activities of two natural isolates of thermophilic lactobacilli, Lactobacillus acidophilus BGRA43 and Lact, delbrueckii BGPF1, and Lact. acidophilus CH2 (Chr. Hansen's strain) and Lact, acidophilus V74 (Visby's strain), were compared. Results revealed that optimal pH for all four proteinases is 6.5, whereas temperature optimum varied among proteinases. Determination of caseinolytic activity done under optimal conditions for each strain revealed that the CH2 and V74 proteinases completely hydrolysed both alpha (s1)-casein and beta -casein, showing very low activity towards kappa -casein. The BGPF1 proteinase completely hydrolysed only beta -casein. The BGRA43 proteinase completely hydrolysed all three casein fractions. The proteolytic activities of whole cells were inhibited by serine proteinase inhibitors, suggesting that all four strains produce serine proteinases. DNA-DNA hybridization and PCR analysis showed that BGPF1 contains the prtB-like proteinase gene. Characterized thermophilic strains BGPF1 and BGRA43 were successfully used as starter cultures for production of yoghurt and acidophilus milk, respectively. PB - Wiley T2 - Journal of Applied Microbiology T1 - Characterization of cell envelope-associated proteinases of thermophilic lactobacilli EP - 130 IS - 1 SP - 123 VL - 90 DO - 10.1046/j.1365-2672.2001.01226.x ER -
@article{ author = "Fira, Đorđe and Kojić, Milan and Banina, Ana and Spasojević, I and Strahinić, Ivana and Topisirović, Ljubiša", year = "2001", abstract = "The proteolytic activities of two natural isolates of thermophilic lactobacilli, Lactobacillus acidophilus BGRA43 and Lact, delbrueckii BGPF1, and Lact. acidophilus CH2 (Chr. Hansen's strain) and Lact, acidophilus V74 (Visby's strain), were compared. Results revealed that optimal pH for all four proteinases is 6.5, whereas temperature optimum varied among proteinases. Determination of caseinolytic activity done under optimal conditions for each strain revealed that the CH2 and V74 proteinases completely hydrolysed both alpha (s1)-casein and beta -casein, showing very low activity towards kappa -casein. The BGPF1 proteinase completely hydrolysed only beta -casein. The BGRA43 proteinase completely hydrolysed all three casein fractions. The proteolytic activities of whole cells were inhibited by serine proteinase inhibitors, suggesting that all four strains produce serine proteinases. DNA-DNA hybridization and PCR analysis showed that BGPF1 contains the prtB-like proteinase gene. Characterized thermophilic strains BGPF1 and BGRA43 were successfully used as starter cultures for production of yoghurt and acidophilus milk, respectively.", publisher = "Wiley", journal = "Journal of Applied Microbiology", title = "Characterization of cell envelope-associated proteinases of thermophilic lactobacilli", pages = "130-123", number = "1", volume = "90", doi = "10.1046/j.1365-2672.2001.01226.x" }
Fira, Đ., Kojić, M., Banina, A., Spasojević, I., Strahinić, I.,& Topisirović, L.. (2001). Characterization of cell envelope-associated proteinases of thermophilic lactobacilli. in Journal of Applied Microbiology Wiley., 90(1), 123-130. https://doi.org/10.1046/j.1365-2672.2001.01226.x
Fira Đ, Kojić M, Banina A, Spasojević I, Strahinić I, Topisirović L. Characterization of cell envelope-associated proteinases of thermophilic lactobacilli. in Journal of Applied Microbiology. 2001;90(1):123-130. doi:10.1046/j.1365-2672.2001.01226.x .
Fira, Đorđe, Kojić, Milan, Banina, Ana, Spasojević, I, Strahinić, Ivana, Topisirović, Ljubiša, "Characterization of cell envelope-associated proteinases of thermophilic lactobacilli" in Journal of Applied Microbiology, 90, no. 1 (2001):123-130, https://doi.org/10.1046/j.1365-2672.2001.01226.x . .