Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp.
Аутори
Tomić, KatarinaŠokarda Slavić, Marinela
Kojić, Milan
Stanisavljević, Nemanja
Nikolić, Stefan
Vujčić, Zoran
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
One of the most abundant natural polymers with multidimensional and multifaceted application is starch. Due to energy fuel sustainability concern, the world is focusing on renewable energy including energy from renewable biological materials like starch1. The importance of the enzymatic hydrolysis of granular starch below the temperature of gelatinization has been well recognized, mainly due to energy savings and the effective utilization of biomass, which reduces the overall cost of starch processing2. A new α-amylase gene (Amy35) was cloned from newly isolated thermophilic Anoxybacillus sp. ST4 and expressed in Escherichia coli. The purified recombinant α-amylase had an wide pH optimum range from 4.5 to 8.5 and optimum temperature of 75°C. The enzyme retained 95% of its activity after 3h of incubation at 50 and 60°C. Hydrolysis rates of potato, horseradish and corn starches, at 1% concentration were 20, 70 and 65%, respectively, in a period of 16 h. Analysis of the enzyme properties ...proved its high efficacy for the digestion of diverse raw starches below gelatinization temperature and, therefore, its potential commercial value for use as an industrial enzyme.
Кључне речи:
α-amylase / Anoxybacillus sp. / starch processingИзвор:
Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia, 2022, 147-Издавач:
- University of Belgrade - Faculty of Chemistry
- Serbian Biochemical Society
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200288 (Иновациони центар Хемијског факултета у Београду доо) (RS-MESTD-inst-2020-200288)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200042 (Универзитет у Београду, Институт за молекуларну генетику и генетичко инжењерство) (RS-MESTD-inst-2020-200042)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200026 (Универзитет у Београду, Институт за хемију, технологију и металургију - ИХТМ) (RS-MESTD-inst-2020-200026)
Институција/група
IHTMTY - CONF AU - Tomić, Katarina AU - Šokarda Slavić, Marinela AU - Kojić, Milan AU - Stanisavljević, Nemanja AU - Nikolić, Stefan AU - Vujčić, Zoran PY - 2022 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/5917 AB - One of the most abundant natural polymers with multidimensional and multifaceted application is starch. Due to energy fuel sustainability concern, the world is focusing on renewable energy including energy from renewable biological materials like starch1. The importance of the enzymatic hydrolysis of granular starch below the temperature of gelatinization has been well recognized, mainly due to energy savings and the effective utilization of biomass, which reduces the overall cost of starch processing2. A new α-amylase gene (Amy35) was cloned from newly isolated thermophilic Anoxybacillus sp. ST4 and expressed in Escherichia coli. The purified recombinant α-amylase had an wide pH optimum range from 4.5 to 8.5 and optimum temperature of 75°C. The enzyme retained 95% of its activity after 3h of incubation at 50 and 60°C. Hydrolysis rates of potato, horseradish and corn starches, at 1% concentration were 20, 70 and 65%, respectively, in a period of 16 h. Analysis of the enzyme properties proved its high efficacy for the digestion of diverse raw starches below gelatinization temperature and, therefore, its potential commercial value for use as an industrial enzyme. PB - University of Belgrade - Faculty of Chemistry PB - Serbian Biochemical Society C3 - Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia T1 - Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp. SP - 147 UR - https://hdl.handle.net/21.15107/rcub_cer_5917 ER -
@conference{ author = "Tomić, Katarina and Šokarda Slavić, Marinela and Kojić, Milan and Stanisavljević, Nemanja and Nikolić, Stefan and Vujčić, Zoran", year = "2022", abstract = "One of the most abundant natural polymers with multidimensional and multifaceted application is starch. Due to energy fuel sustainability concern, the world is focusing on renewable energy including energy from renewable biological materials like starch1. The importance of the enzymatic hydrolysis of granular starch below the temperature of gelatinization has been well recognized, mainly due to energy savings and the effective utilization of biomass, which reduces the overall cost of starch processing2. A new α-amylase gene (Amy35) was cloned from newly isolated thermophilic Anoxybacillus sp. ST4 and expressed in Escherichia coli. The purified recombinant α-amylase had an wide pH optimum range from 4.5 to 8.5 and optimum temperature of 75°C. The enzyme retained 95% of its activity after 3h of incubation at 50 and 60°C. Hydrolysis rates of potato, horseradish and corn starches, at 1% concentration were 20, 70 and 65%, respectively, in a period of 16 h. Analysis of the enzyme properties proved its high efficacy for the digestion of diverse raw starches below gelatinization temperature and, therefore, its potential commercial value for use as an industrial enzyme.", publisher = "University of Belgrade - Faculty of Chemistry, Serbian Biochemical Society", journal = "Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia", title = "Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp.", pages = "147", url = "https://hdl.handle.net/21.15107/rcub_cer_5917" }
Tomić, K., Šokarda Slavić, M., Kojić, M., Stanisavljević, N., Nikolić, S.,& Vujčić, Z.. (2022). Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp.. in Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia University of Belgrade - Faculty of Chemistry., 147. https://hdl.handle.net/21.15107/rcub_cer_5917
Tomić K, Šokarda Slavić M, Kojić M, Stanisavljević N, Nikolić S, Vujčić Z. Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp.. in Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia. 2022;:147. https://hdl.handle.net/21.15107/rcub_cer_5917 .
Tomić, Katarina, Šokarda Slavić, Marinela, Kojić, Milan, Stanisavljević, Nemanja, Nikolić, Stefan, Vujčić, Zoran, "Cloning and characterization of new raw starch digestion α-amylase from thermophilic Anoxybacillus sp." in Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia (2022):147, https://hdl.handle.net/21.15107/rcub_cer_5917 .