Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 11Citation - Scopus: 16Purification and Biochemical Characterization of a Novel Thermostable Serine Protease From Geobacillus Sp. Gs53(Springer, 2021) Şanlı Mohamed, Gülşah; Güracar Baykara, Seden; Sürmeli, YusufProteases account for approximately 60% of the enzyme market in the world, and they are used in various industrial applications including the detergent industry. In this study, production and characterization of a novel serine protease of thermophilic Geobacillus sp. GS53 from Balcova geothermal region, Izmir, Turkey, were performed. The thermostable protease was purified through ammonium sulfate precipitation and anion-exchange chromatography. The results showed that the protease had 137.8 U mg(-1) of specific activity and optimally worked at 55 C-o and pH 8. It was also active in a broad pH (4-10) and temperature (25-75 degrees C) ranges. The protease was highly stable at 85 degrees C and demonstrated relative stability at pH 4, 7, and 10. Also, the enzyme had high stability against organic solvents and surfactants; enzyme relative activity did not decrease below 81% upon preincubation for 10 min. Ca2+, Cu2+, and Zn2+ ions slightly induced protease activity. The protease was highly specific to casein, skim milk, Hammerstein casein, and BSA substrates. These results revealed that the protease might have a potential effect in a variety of industrial fields, especially the detergent industry, because of its high thermostability and stability to surfactants.Article Citation - WoS: 18Citation - Scopus: 23A Thermophilic ?-L From Geobacillus Vulcani Gs90: Heterologous Expression, Biochemical Characterization, and Its Synergistic Action in Fruit Juice Enrichment(Springer, 2018) İlgü, Hüseyin; Sürmeli, Yusuf; Şanlı Mohamed, Gülşahα-l-Arabinofuranosidases with an orchestral action of xylanolytic enzymes degrades the xylan in plant cell wall. In this study, heterologous expression, biochemical characterization, and synergistic action of α-l-Arabinofuranosidase from previously identified.Geobacillus vulcani GS90 (GvAbf) was investigated. The recombinant α-l-Arabinofuranosidase was overexpressed in Escherichia coli BL21 (λDE) and purified via His-tag Ni-affinity and size-exclusion chromatography. Optimum activity of the purified α-l-Arabinofuranosidase was obtained at pH 5 and at 70 °C. The GvAbf was active in a broad pH and temperature ranges; pH 4–9 and 30–90 °C, respectively. In addition, it retained most of its activity after an hour incubation at 70 °C and remained relatively stable at pH 3–6. GvAbf was quite stable against various metal ions. The kinetic parameters of GvAbf was obtained as Vmax and Km; 200 U/mg and 0.2 mM with p-nitrophenyl-α-l-arabinofuranoside and 526 U/mg and 0.1 mM with sugar beet arabinan, respectively. The synergistic action of GvAbf was studied with commercially available xylanase on juice enrichment of apples, grapes, oranges, and peaches. The best juice enrichment in terms of clarity, reducing sugar content, and yield, was achieved with GvAbf and xylanase together compared to treatment with xylanase and GvAbf alone in all fruits. The treatment with GvAbf and xylanase together lead to an increased juice yield by 26.56% (apple), 30.88% (grape), 40.00% (orange) and 32.20% (peach) as well as having a significant effect on juice clarity by an increase of % transmittance 47.26, 25.98, 41.77, and 44.97, respectively. The highest reducing sugar level of fruit juices also obtained with GvAbf and xylanase together compared to treatment with xylanase and GvAbf alone in all types of fruits. GvAbf and xylanase together as simultaneous synergistic manner may have an exciting potential for application in fruit juice processing.