Bitki örneklerinden seçici gallik asit ayrılması için gallik asit baskılanmış polimerlerin hazırlanması

Bu çalışmada, yaygın olarak kullanılan doğal bir antioksidan olan gallik asidin (GA) moleküler baskılama yöntemi kullanılarak hazırlanan polimerlerle (MIP) bitki örneklerinden seçici ayrılması gerçekleştirilmiştir. Emülsiyon polimerizasyonu ile hazırlanan polimerler çeşitli yöntemlerle karakterize edilmiştir. GA adsorpsiyonunun optimizasyon çalışmaları, pH 3,5 ortamında 25°C’de 1,2 mg GA-MIP kullanılarak 60 dk sürenin GA adsorpsiyonu için en uygun koşullar olduğunu göstermiş ve GA adsorpsiyonu adsorpsiyon kinetikleri ve izotermleri ile incelenmiştir. Çalışılan tüm derişimler için IF değerinin 1’den büyük olması GA-MIP’lerin baskılanmamış polimerlere (GA-NIP) kıyasla daha fazla GA adsorpladığını kanıtlamaktadır. Ayrıca, IF değerinin GA derişimiyle ters orantılı olarak azalması spesifik olmayan etkileşimlerden kaynaklanmaktadır. MIP’lerin seçiciliğini belirlemek amacıyla GA analogları kullanılarak yarışmalı adsorpsiyon çalışmaları yapılmış ve GA ve analoglarının miktarları yüksek performanslı sıvı kromatografisi ile analiz edilmiştir. Tüm bağıl seçicilik katsayılarının 1’den büyük olması GA-MIP’lerin baskılanmamış polimerlere kıyasla GA’yı tüm analoglarından daha fazla adsorpladığını göstermektedir. Yeşil çay, siyah çay ve karanfil örnekleri ile yapılan gerçek örnek çalışmaları sonucunda en etkin GA adsorpsiyonu ve geri alımının karanfil örnekleriyle elde edildiği belirlenmiştir. HPLC kromatogramları incelendiğinde, GA’nın etkin ve seçici olarak MIP’lerden geri alındığı belirlenmiştir.In this study, gallic acid (GA) which is a commonly used natural antioxidant has been separated from plant samples with the polymers (MIP) prepared by using molecular imprinting technique. The polymers produced by emulsion polymerization has been characterized by several methods. Optimization studies for the adsorption of GA has been indicated that pH 3.5 medium at 25°C with using 1,2 mg GA-MIP for 60 min period are optimum conditions for GA adsorption and GA adsorption has been investigated by adsorption kinetics and isotherms. IF values being more than 1 for all working concentrations have demonstrated that GA-MIPs adsorbed more GA in regard to non-imprinted polymers (GA-NIPs). However, decreasing IF values inversely proportional with increasing concentration are due to the non-specific interactions. For the identification of MIPS’ selectivity, competitive adsorption studies have been carried out with using GA analogues and amounts of GA and its analogues have been analyzed with high performance liquid chromatography (HPLC). All relative selectivity coefficients greater than 1 have showed that GA-MIPs adsorbed more GA than its analogues as regards to GA-NIPs. As a result of real sample studies with green tea, black tea and clove samples, most efficient GA adsorption and recovery has been achieved with clove samples. It is indicated by analyzing HPLC chromatograms, GA has been recovered effectively and selectively from MIPs

Chitosan Co-polymeric nanostructures for catalase immobilization

WOS: 000458222500011Catalase is an industrial enzyme used in different areas including medical, textile, food and pharmaceutic industries. In the study, synthetic-natural copolymer in nanosize was synthesized using 2-hydroxyethyl methacrylate (HEMA) as a synthetic material and chitosan (CTS) as a natural material. Immobilized metal-chelate affinity chromatography (IMAC) material was prepared by chelating Cu(II) ions onto p(HEMA-CTS) nanostructures. Characterization studies such as Zeta sizer analysis, Fourier transform infra-red (FTIR) spectroscopy, scanning electron microscopy (SEM), and thermal gravimetric analysis (TGA) were performed during the preparation of IMAC nanostructures. The effects of some parameters (time, polymer amount, pH, initial catalase concentration, ionic strength and temperature) were identified and optimum immobilization conditions were determined as 75 min, 0.1 mg p(HEMA-CTS)-Cu, pH 6.0, and 25 degrees C. Maximum amount of immobilized catalase was detected as 11.29 g/g p(HEMA-CTS)-Cu. Immobilized catalase was desorbed successfully and it was detected that p(HEMA-CTS)-Cu nanostructures can be used repeatedly in catalase immobilization. Immobilization changed optimum temperature value from 37 degrees C to 25 degrees C while it did not change the optimum pH for catalase activity. Furthermore, it was detected that kinetic parameters of catalase changed by immobilization. Finally, operational and storage stabilities of immobilized catalase were investigated.Aksaray University Research Fund [2016-016]This work was supported by the Aksaray University Research Fund [Grant number 2016-016]

Cryogel disks for lactase immobilization and lactose-free milk production

This study aims to optimize lactase immobilization onto Fe-chelated cryogel disks. p(AAm-HEMA) cryogel disks were prepared by free radical polymerization and chelated with Fe ions to prepare IMAC material. The lactase immobilization was optimized after characterization by physical analysis. Lactase activity assays were performed with ONPG and lactose substrates. The maximum amount of immobilized lactase was determined as 107.2 ± 4.3 mg/g at 1.5 mg/mL and pH 4.5. The optimum pH of immobilized lactase was determined as pH 5.0, and the immobilized lactase showed notably higher catalytic activity at pH 3.0 compared to free lactase. The optimum temperature of lactase shifted from 50 °C to 60 °C, and the immobilized lactase presented higher activity at 60 °C and 65 °C than the free lactase. Higher thermal activities were achieved for all temperature values after immobilization. The catalytic effectiveness of lactase was not affected, and similar KM values were calculated for lactose. The immobilized lactase lost 29.2% of its initial activity at the end of 70 days, and preserved 64.9% of initial activity after 25-runs. All lactose in milk was hydrolysed by lactase immobilized cryogel disks in 5 h. The lactase immobilized cryogel disks present encouraging opportunities for lactose-free milk preparation in food industry

Effects of dietary Ferula elaeochytris root powder concentrations on haematology, serum biochemical parameters, spermatozoa parameters, and oxidative status in tissues of males goldfish (Carassius auratus)

This study evaluates the effects of Ferula elaeochytris, a traditional medicinal herb, root powder (FRP) concentrations (0, 0.5%, 1%, 0.5% and 1%) on serum biochemical parameters, hematological profiles, oxidative stress conditions in liver, muscle, gonad, testicular and stripped spermatozoa, and also spermatozoa parameters of adult male goldfish (Carassius auratus). To the best of our knowledge, this is the first time that the effects of FRP on these parameters as being associated with its essential oil contents have been determined. Some important bioactive compounds such as such as 14-beta-H-Pregna, alpha-curcumene, limonene have been determined in FRP. Following a 60-day feeding trial, blood samples were taken and then females were introduced to tanks together with changing photoperiod and water temperature for 10 days to promote spermiation. Results showed that RBC, haemoglobin, and haematocrit levels increased in 1% of FRP fed fish compared control group (P 0.05). Also serum total protein and albumin levels in this group slightly increased (P 0.05). However, blood parameters were negatively affected in 1% of FRP. Spermatozoa parameters dramatically decreased, even spermiation success could not be achieved in some fish in fish fed with 1% of FRP. Also, 1% of FRP in diet induced oxidative stress conditions in the tissues of this group. These conditions in gonad had a different pattern than those in liver in muscle. The results revealed that dietary 1% of FRP could be an advantageous additive while FRP at levels of >0.5% in diet was useless for or has deleterious effects on fish health and reproduction. Based on these results, we conclude that a supplement suitable concentration and analysis of major compounds of medicinal herbs which would use should be taken into consideration when planning to use them in fish diets

Oxime-functionalized cryogel disks for catalase immobilization

WOS: 000435056900092PubMed: 29626600Catalase is a protective enzyme against oxidative stress and converts hydrogen peroxide into water and molecular oxygen. In the current study, catalase immobilization was applied onto the oxime-functionalized cryogel disks. Cryogel disks were produced by free radical polymerization. After cutting as circular disks, oxime ligand (4-biphenylchloroglyoxime, BPCGO) was attached and oxime-functionalized cryogel disks were obtained. After optimization of several immobilization parameters such as pH, initial catalase concentration, temperature and ionic strength, maximum catalase load was detected as 261.7 +/- 11.2 mg/g for cryogel disk at pH 5.0. Activity studies indicated that immobilization enhanced the enzyme activity in basic pH region, the temperature range of 15-35 degrees C and at ionic strengths between 0.2 and 1.0 M NaCI. Km was detected as 9.9 and 11.0 mM and V-max was 357.1 and 769.2 mu mol min(-1) for free and immobilized catalase, respectively. k(cat) and Km/k(cat) values showed that immobilization enhanced the catalytic efficiency. Storage stability experiments demonstrated that immobilization increased the usability period. Furthermore, catalase desorption was achieved by 1.0 M NaSCN at pH 8.0 successfully and catalase adsorption capacity of oxime-functionalized cryogel disk was decreased by 9.9% at the end of 5 adsorption-desorption cycle

Total antioxidant capacity, catalase activity, and lipid peroxidation changes in seminal plasma of sex-reversed female and male rainbow trout (Oncorhynchus mykiss) during spawning season

WOS: 000384628200015PubMed: 27474236The advantages of gender-related characteristics are used in aquaculture practice to improve production. For instance, all-female stocic is preferable than mixed or all-male stock in salmonid culture. The most effective way to obtain all-female populations is the using of sex-reversed (SR) female trouts, genotypically female but phenotypically male, by masculinizing androgen hormones as breeders in artificial insemination. This study was conducted to evaluate changes in the total antioxidant capacity (TAC), protein concentration, catalase (CAT) activity, lipid peroxidation level (LPO; malondialdehyde), and Fourier transform infrared spectra of seminal plasma of SR female and normal (N) male trouts during the spawning season. Seminal plasma TAC values of N male and SR female trouts were determined as 0.015 +/- 0.004 and 0.116 +/- 0.033 mM of Trolox equivalents, respectively, in the middle of the spawning season. Some regions related to aromatic rings in seminal plasma Fourier transform infrared spectra of SR female trouts differed from N male trouts were indicated to the higher TAC values. At the middle of the spawning season, protein concentrations were determined as 569.5 +/- 139.4 mg/dL in SR female trouts and 663 +/- 22.7 mg/dL in N male trouts. LPO levels in seminal plasma of N male trouts varied from 46.33 +/- 12.05 x 10(-3) to 270.02 +/- 70.64 x 10(-3) nmolimg protein, whereas from 13.87 +/- 4.98 x 10(-3) to 48.49 +/- 1731 x 10(-3) nmolimg protein in SR female trouts throughout the spawning. CAT activities of seminal plasma in N male trouts ranged from 038 +/- 0.26 to 0.47 +/- 0.32 Ming protein, whereas those values in SR female trouts varied between 0.21 +/- 0.10 and 0.43 +/- 0.15 kU/mg protein. Moreover, there were the pairwise significant correlations among all variables except between CAT and TAC (P > 0.05). Remarkable correlations were found between LPO-protein (r = -0.922, P < 0.05, n = 190), LPO-TAC (r = 0.859, P < 0.05, n = 98), and TAC protein (r = +0.879, P < 0.05, n = 98). Similar to seminal plasma of N male trouts, TAC values, protein concentrations, and CAT activities in seminal plasma of SR female trouts have shown decline, whereas LPO levels increased toward the end of the spawning seasons. Seminal plasmas of SR female trouts were characterized by higher protein concentrations and TAC values and lower LPO levels than that from N male trouts.Mugla Sitki Kocman University Research Fund [BAP 2012/92]; Scientific and Technical Research Council of Turkey (TUBITAK) [1130606]This study has been financially supported by Mugla Sitki Kocman University Research Fund (Grant number: BAP 2012/92) and The Scientific and Technical Research Council of Turkey (TUBITAK) (Grant number: 1130606). The authors also would like to thank personnel from the fish farm manager and the hatchery manager Ersin Celik for technical assistance during sampling