Food Engineering / Gıda Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/12
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Article Citation - WoS: 3Citation - Scopus: 5Production of Food Grade Ss-Galactosidase From Artisanal Yogurt Strains(Taylor and Francis Ltd., 2010) Tarı, Canan; Üstok, Fatma Işık; Harsa, ŞebnemSuperior artisanal isolates of thermophilic lactic acid bacteria producing high lactic acid and β-galactosidase were isolated from traditional Turkish yogurt samples from the Toros mountain region from a highly bio-diverse environment. A full factorial statistical design, with the factors of types of strains and medium formulations under static and agitation conditions, were applied to investigate the effects on β-galactosidase and lactic acid production. Streptococcus thermophilus 95/2 and Lactobacillus delbrueckii subsp. thermophilus 77 exhibited remarkable potential as promising starter culture candidates valuable to various applications in the dairy industry. The efficiency of cell disruption methods was investigated on the extraction of intracellular β-galactosidase enzyme. Lysozyme enzyme treatment was determined as the most effective method, which resulted in approximately 1.5 and 10 times higher enzyme activity than glass bead and homogenization treatment, respectively. © Taylor & Francis Group, LLC.Article Citation - WoS: 48Citation - Scopus: 59Biochemical and Thermal Properties of Ss-Galactosidase Enzymes Produced by Artisanal Yoghurt Cultures(Elsevier Ltd., 2010) Üstok, Fatma Işık; Tarı, Canan; Harsa, Şebnemβ-Galactosidases, produced by pure and mixed cultures of Streptococcus thermophilus 95/2 (St 95/2) and Lactobacillus delbrueckii ssp bulgaricus 77 (Lb 77) isolated from the Toros mountain region of Turkey, were characterised with respect to their biochemical and thermal properties. Optimum pH and temperature for maximum activity were determined and these enzymes were stable in the pH range 7-9 and in the temperature range 20-37 °C, retaining 80-90% of their initial activities. The inactivation energies of β-galactosidase from Lb 77, St 95/2 and mixed culture (Lb 77 and St 95/2) were 51.3, 44.0 and 48.3 kcal mol-1, respectively. Moreover, thermodynamic (ΔG, ΔS, ΔH) and kinetic constants (Km and Vmax) were determined and effects of metal ions were investigated. As a result, these enzymes could be considered as potential candidates for lactose hydrolysis of milk and milk products. © 2009 Elsevier Ltd. All rights reserved.Article Citation - WoS: 19Citation - Scopus: 22Optimization of the Associative Growth of Novel Yoghurt Cultures in the Production of Biomass, Ss-Galactosidase and Lactic Acid Using Response Surface Methodology(Elsevier Ltd., 2009) Tarı, Canan; Üstok, Fatma Işık; Harsa, Hayriye ŞebnemThe associative growth of Streptococcus thermophilus 95/2 (St 95/2) and Lactobacillus delbrueckii ssp. bulgaricus 77 (Lb 77) isolated from the Toros mountain region of Turkey was investigated with respect to lactic acid, biomass and β-galactosidase enzyme production using response surface methodology (RSM). The ratio (St 95/2:Lb 77) of the strains and media formulation had significant effect on all responses (p < 0.001). The predicted enzyme activity (2.14 U mL-1), lactic acid (22.50 g L-1) and biomass (7.11 g L-1) production at optimum conditions were very close to the actual experimental values (2.14 U mL-1, 22.94 g L-1 and 7.86 g L-1, respectively). The optimum conditions were to use these cultures in a ratio of 1.66:1.62 (St 95/2:Lb 77) in a medium containing whey (5%), corn steep liquor (4%), potassium phosphate (2%) and peptone (2%) at 43 °C for 8 h. The associative growth provided 6.4% and 39% more β-galactosidase activity and 8.73% and 44% more lactic acid compared with the results obtained using pure St 95/2 and Lb 77 strains, respectively.Article Citation - WoS: 52Citation - Scopus: 62Solid-State Production of Polygalacturonase by Aspergillus Sojae Atcc 20235(Elsevier Ltd., 2007) Üstok, Fatma Işık; Tarı, Canan; Göğüş, NihanThe effect of solid substrates, inoculum and incubation time were studied using response surface methodology (RSM) for the production of polygalacturonase enzyme and spores in solid-state fermentation using Aspergillus sojae ATCC 20235. Two-stage optimization procedure was applied using D-optimal and face-centered central composite design (CCD). Crushed maize was chosen as the solid substrate, for maximum polygalacturonase enzyme activity based on D-optimal design. Inoculum and incubation time were determined to have significant effect on enzyme activity and total spore (p < 0.01) based on the results of CCD. A second order polynomial regression model was fitted and was found adequate for individual responses. All two models provided an adequate R2 of 0.9963 (polygalacturonase) and 0.9806 (spores) (p < 0.001). The individual optimum values of inoculum and incubation time for maximum production of the two responses were 2 × 107 total spores and 5-6 days. The predicted enzyme activity (30.55 U/g solid) and spore count (2.23 × 107 spore/ml) were very close to the actual values obtained experimentally (29.093 U/g solid and 2.31 × 107 spore/ml, respectively). The overall optimum region considering the two responses together, overlayed with the individual optima. Solid-state fermentation provided 48% more polygalacturonase activity compared to submerged fermentation under individually optimized conditions.Article Citation - WoS: 11Citation - Scopus: 16Partial Purification of Hen Egg White Lysozyme by Ethanol Precipitation Method and Determination of the Thermal Stability of Its Lyophilized Form(Türkiye Klinikleri Journal of Medical Sciences, 2007) Gemili, Seyhun; Umdu, Emin Selahattin; Yaprak, Nilgün; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Mecitoğlu Güçbilmez, Çiğdem; Altınkaya, Sacide; Yemenicioğlu, AhmetLysozyme was partially purified from hen egg white by precipitation of non-lysozyme protein impurities during incubation in the prence of ethanol. The thermal stability of the obtained partially purified enzyme was also characterized. The incubation of diluted egg white for 2-8 h in the presence of 20% ethanol was not very effective for the partial purification of lysozyme by precipitation of major egg white proteins; however, 4- to 6-h or 6-h to 8-h incubation of diluted egg white in the presence of 30% and 40% ethanol could be employed more effectively for partial purification of lysozyme. Without applying the incubation period, the highest specific activity was obtained by the treatment of egg white with 40% ethanol. Thus, ethanol at this concentration could be used for a continuous process of partial purification. For batch lysozyme purification, on the other hand, incubation in the presence of 30% ethanol was more appropriate. The activities and protein contents of dialyzed and lyophilized enzymes obtained by 6 h-incubation in the presence of 20%, 30%. and 40% ethanol precipitations were 1878, 6669, and 6115 U/mg powder, and 0.98, 0.90, and 0.93 mg protein per mg powder, respectively. The ranges of thermal inactivation parameters, such as D (D80°C = 29.2-59 min, D90°c = 8.8-21 min) and z (Z80-90°c = 17.4-22.3 °C) values of the enzyme, clearly indicated the moderate and variable heat stability of lyophilized lysozymes obtained from different batches of egg white.