Tarı, Canan

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Name Variants
Tarı, C
Tarı, C.
Tari, Canan
Tari, C.
Tari, C
Job Title
Email Address
Main Affiliation
03.08. Department of Food Engineering
Status
Former Staff
Website
Scopus Author ID
Turkish CoHE Profile ID
Google Scholar ID
WoS Researcher ID

Sustainable Development Goals

NO POVERTY1
NO POVERTY
0
Research Products
ZERO HUNGER2
ZERO HUNGER
7
Research Products
GOOD HEALTH AND WELL-BEING3
GOOD HEALTH AND WELL-BEING
0
Research Products
QUALITY EDUCATION4
QUALITY EDUCATION
1
Research Products
GENDER EQUALITY5
GENDER EQUALITY
0
Research Products
CLEAN WATER AND SANITATION6
CLEAN WATER AND SANITATION
10
Research Products
AFFORDABLE AND CLEAN ENERGY7
AFFORDABLE AND CLEAN ENERGY
11
Research Products
DECENT WORK AND ECONOMIC GROWTH8
DECENT WORK AND ECONOMIC GROWTH
4
Research Products
INDUSTRY, INNOVATION AND INFRASTRUCTURE9
INDUSTRY, INNOVATION AND INFRASTRUCTURE
15
Research Products
REDUCED INEQUALITIES10
REDUCED INEQUALITIES
0
Research Products
SUSTAINABLE CITIES AND COMMUNITIES11
SUSTAINABLE CITIES AND COMMUNITIES
0
Research Products
RESPONSIBLE CONSUMPTION AND PRODUCTION12
RESPONSIBLE CONSUMPTION AND PRODUCTION
8
Research Products
CLIMATE ACTION13
CLIMATE ACTION
12
Research Products
LIFE BELOW WATER14
LIFE BELOW WATER
2
Research Products
LIFE ON LAND15
LIFE ON LAND
0
Research Products
PEACE, JUSTICE AND STRONG INSTITUTIONS16
PEACE, JUSTICE AND STRONG INSTITUTIONS
0
Research Products
PARTNERSHIPS FOR THE GOALS17
PARTNERSHIPS FOR THE GOALS
0
Research Products
Documents

34

Citations

1374

h-index

19

This researcher does not have a WoS ID.
Scholarly Output

51

Articles

37

Views / Downloads

48110/29333

Supervised MSc Theses

8

Supervised PhD Theses

2

WoS Citation Count

1137

Scopus Citation Count

1360

Patents

0

Projects

4

WoS Citations per Publication

22.29

Scopus Citations per Publication

26.67

Open Access Source

50

Supervised Theses

10

JournalCount
Journal of Biotechnology4
Biochemical Engineering Journal3
GIDA3
Turkish Journal of Biology2
Applied Microbiology and Biotechnology2
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Scholarly Output Search Results

Now showing 1 - 10 of 51
  • Article
    Citation - WoS: 52
    Citation - Scopus: 62
    Solid-State Production of Polygalacturonase by Aspergillus Sojae Atcc 20235
    (Elsevier Ltd., 2007) Üstok, Fatma Işık; Tarı, Canan; Göğüş, Nihan
    The 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: 61
    Citation - Scopus: 75
    Optimization of Biomass, Pellet Size and Polygalacturonase Production by Aspergillus Sojae Atcc 20235 Using Response Surface Methodology
    (Elsevier Ltd., 2007) Tarı, Canan; Göğüş, Nihan; Tokatlı, Figen
    A two-step optimization procedure using central composite design with four factors (concentrations of maltrin and corn steep liquor (CSL), agitation speed and inoculation ratio) was used in order to investigate the effect of these parameters on the polygalacturonase (PG) enzyme activity, mycelia growth (biomass) and morphology (pellet size) of Aspergillus sojae ATCC 20235. According to the results of response surface methodology (RSM), initial concentrations of maltrin and CSL and agitation speed were significant (p < 0.05) on both PG enzyme production and biomass formation. As a result of this optimization, maximum PG activity (13.5 U/ml) was achievable at high maltrin (120 g/l), at low CSL (0 g/l), high agitation speed (350 rpm) and high inoculation ratio (2 × 107 total spore). Similarly, maximum biomass (26 g/l) could be obtained under the same conditions with only the difference for higher level of CSL requirement. The diameter of pellets in all optimization experiments ranged between 0.05 and 0.76 cm. The second optimization step improved the PG activity by 74% and the biomass by 40%.
  • Article
    Citation - WoS: 14
    Citation - Scopus: 12
    Enhanced Production of Exo-Polygalacturonase From Agro-Based Products by Aspergillus Sojae
    (North Carolina University, 2011) Büyükkileci, Ali Oğuz; Tarı, Canan; Fernandez-Lahore, Marcello
    Aspergillus sojae has been previously shown to produce exo-polygalacturonase (exo-PG) in synthetic media, where the potential of the organism to utilize agricultural substrates was not considered so far. In this study, the utilization of agro-based products was taken into account in the enhanced production of exo-PG using an A. sojae mutant by applying statistical design methods. Complex sources (orange peel, wheat bran, and corn meal), simple sugar sources (glucose, maltrin, and sugar beet syrup), and two phosphate salts were screened using D-optimal design method. Orange peel yielded the highest exo-PG activity with all simple sugars and phosphate sources. According to the results of response surface methodology (RSM), the optimum concentrations of orange peel, sugar beet syrup, and (NH 4) 2SO 4 were found to be 10, 60, and 8 g L -1, respectively. The exo-PG activity under these conditions was 145.4 U m L -1 in shake flask cultures. In bioreactor studies enzyme production was induced at low pH values; thus highest production was obtained under uncontrolled pH conditions, in which the pH dropped to 2.0 in 72 h. As a result high exo-PG could be produced by an A. sojae mutant using a cost-effective medium containing agro-industrial substrates. Another important advantageous outcome was the low optimal pH, which is especially desired in industrial fermentations prone to contamination problems. In fact this highlights the easy adaptation of this fermentation to industrial scales.
  • Article
    Citation - WoS: 45
    Citation - Scopus: 52
    Biochemical and Thermal Characterization of Crude Exo-Polygalacturonase Produced by Aspergillus Sojae
    (Elsevier Ltd., 2008) Tarı, Canan; Doğan, Nergiz; Göğüş, Nihan
    Crude exo-polygalacturonase enzyme (produced by Aspergillus sojae), significant for industrial processes, was characterized with respect to its biochemical and thermal properties. The optimum pH and temperature for maximum crude exo-polygalacturonase activity were pH 5 and 55 °C, respectively. It retained 60-70% of its activity over a broad pH range and 80% of its initial activity at 65 °C for 1 h. The thermal stability study indicated an inactivation energy of Ed = 152 kJ mol-1. The half lives at 75 and 85 °C were estimated as 3.6 and 1.02 h, respectively. Thermodynamic parameters, ΔH*, ΔS* and ΔG*, were determined as a function of temperature. The kinetic constants Km and Vmax, using polygalacturonic acid as substrate, were determined as 0.424 g l-1 and 80 μmol min-1, respectively. SDS-PAGE profiling revealed three major bands with molecular weights of 36, 53 and 68 kDa. This enzyme can be considered as a potential candidate in various applications of waste treatment, in food, paper and textile industries.
  • Article
    Citation - WoS: 29
    Citation - Scopus: 29
    Microbial Strain Improvement for Enhanced Polygalacturonase Production by Aspergillus Sojae
    (Springer Verlag, 2014) Heerd, Doreen; Tarı, Canan; Fernandez Lahore, Marcelo
    Strain improvement is a powerful tool in commercial development of microbial fermentation processes. Strains of Aspergillus sojae which were previously identified as polygalacturonase producers were subjected to the cost-effective mutagenesis and selection method, the so-called random screening. Physical (ultraviolet irradiation at 254 nm) and chemical mutagens (N-methyl-N′-nitro-N-nitrosoguanidine) were used in the development and implementation of a classical mutation and selection strategy for the improved production of pectic acid-degrading enzymes. Three mutation cycles of both mutagenic treatments and also the combination of them were performed to generate mutants descending from A. sojae ATCC 20235 and mutants of A. sojae CBS 100928. Pectinolytic enzyme production of the mutants was compared to their wild types in submerged and solid-state fermentation. Comparing both strains, higher pectinase activity was obtained by A. sojae ATCC 20235 and mutants thereof. The highest polygalacturonase activity (1,087.2±151.9 U/g) in solid-state culture was obtained by mutant M3, which was 1.7 times increased in comparison to the wild strain, A. sojae ATCC 20235. Additional, further mutation of mutant M3 for two more cycles of treatment by UV irradiation generated mutant DH56 with the highest polygalacturonase activity (98.8±8.7 U/mL) in submerged culture. This corresponded to 2.4-fold enhanced polygalacturonase production in comparison to the wild strain. The results of this study indicated the development of a classical mutation and selection strategy as a promising tool to improve pectinolytic enzyme production by both fungal strains.
  • Master Thesis
    Studies on Alkaline Protease Production From Bacillus Sp.
    (Izmir Institute of Technology, 2004) Gençkal, Hande; Tarı, Canan
    The aim of this study was optimization of the conditions for the production of alkaline protease from the Bacillus strains coded as L18, L21 and I18, which were isolated from our natural habitats. Additionally, the goal was also to optimize the production of alkaline protease from Bacillus sp. L21 in a new low-cost media formulation by employing design of experiments and response surface methodology. Lastly, the focus was given to the determination of the characteristic properties of the crude alkaline protease of Bacillus sp. L21. The strains L21 and L18 were supplied by İYTE Department of Biology, whereas I18 was supplied by Ege University Department of Biology. These potential alkaline protease producer strains identified as Bacillus sp. were isolated from the products of a leather factory (strains L21 and L18) and from the soil of the Ege University Campus (strain I18). When the effects of environmental conditions on alkaline protease production from strains L21, L18 and I18 were studied, the optimum temperatures were determined as 30 C for strain I18 and 37 C for the strains L18 and L21. Similarly the optimum agitation speeds were 100 rpm for I18 and 180 rpm for L18 and L21. The optimum inoculation ratio was determined as 5% (v/v) for all three strains. The optimum incubation time was determined as 96 hours for the strains I18 and L21 and 125 hours for L18. The optimum initial media pH was estimated as pH 10 for strain L18 and L21. The relative importance of these factors on alkaline protease production was investigated by using a resolution IV fractional factorial design with single replicate of treatment combinations of four factors (soybean meal, corn steep liquor, CaCl2, Tween 80). Soybean meal, maltose, Tween 80 concentrations and initial pH were found to significantly influence the alkaline protease production. For obtaining the mutual interaction between the variables and optimizing these variables, Box-Behnken design and central composite design (CCD) using response surface methodology was employed. The neutral pH values of the medium and Tween 80 around its maximum level has a positive effect on proteolytic activity. Additionally, 4 sets of validation experiments were employed. The validation experiment, which state soybean meal, maltose, Tween 80 and pH as 2.5 g/L, 15 g/L, 0.35 g/L and 8.5, respectively, yielded an actual protease activity of 294.3 U/mL, where the model estimated a value of 338 U/mL. The Box-Behnken design and validation experiments were not sufficient to determine the true optimum values for the significant factors because of the saddle nature of the response surfaces. Therefore pH and Tween 80 were kept constant and a central composite design with two factors (soybean meal and maltose concentrations) was conducted. The adjusted R2 of the model was 93.3% with an insignificant lack of fit (p value.0.141). The CCD was able to determine the optimum value of soybean meal as 3.0 g/L, however it could be determined for maltose concentration after a set of additional experiments. Consequently, the optimum values of the four factors were determined as 8.0 for pH, 0.35 g/L for Tween 80, 3.0 g/L for soybean meal and 30-40 g/L for maltose concentration. The maximum activity under these conditions was 269.2 U/mL. In the characterization part of this study, the crude alkaline protease of Bacillus sp. L21 displayed a pH optimum of 11.0 and retained about 73-78% of its original activity between pH 4.0 and 11.0 in the stability studies. The optimum temperature for protease activity was found to be 60C and retained about 90% of the original activity even at 80C. By analyzing the thermal stability, the alkaline protease was found to be stable in a temperature range of 30C to 50C but lost about 30% of its activity at 60C after 30 min and 1 hour incubations both in the presence and absence of Ca2+-The protease from strain L21 showed high stability against both 5% and 15% (v/v) concentrations of H2O2 which is a bleaching agent, and retained approximately 82% and 94% of its activity, respectively, therefore, the present alkaline protease is thought to be a bleach-stable enzyme, so that it can be used in detergent formulations. There was no inhibitory effect observed from EDTA that further show that the enzyme is not a metalloprotease. However, PMSF (phenylmethylsulphonyl fluoride) strongly inhibited the protease activity, suggesting that the enzyme is a serine protease. In addition,CaC12 showed inhibitory effect on the enzyme, decreasing the activity to 90% of the control and this can be explained that the enzyme do not require the presence of Ca2+ ions to be active and stable.
  • Article
    Citation - WoS: 28
    Citation - Scopus: 32
    Optimization of the Process Parameters for the Utilization of Orange Peel To Produce Polygalacturonase by Solid-State Fermentation From an Aspergillus Sojae Mutant Strain
    (TUBITAK, 2012) Demir, Hande; Göğüş, Nihan; Tarı, Canan; Heerd, Doreen; Lahore, Marcelo Fernandez
    The effect of orange peel concentration, HCl concentration, incubation time and temperature, and inoculum size on the spore count and activity of polygalacturonase (PG) enzyme produced from Aspergillus sojae M3 by solidstate fermentation was screened using 2k factorial design. Orange peel and HCl concentrations and incubation time were significant factors affecting the responses. Optimum conditions favoring both PG and spore production from Aspergillus sojae M3 were determined as 2% orange peel and 50 mM HCl concentrations at 22 °C and 4.3 days of incubation. An overlay plot was constructed for use as a practical chart for production of high enzyme activity (>35.0 U/g substrate) and spore count (9.0 × 108 to 2.0 × 109 spore/mL) by superimposing the contours of PG activity and spore count responses. The accuracy and reliability of the constructed models on the responses was validated with the maximum calculated error rate between the predicted and actual activities at 14.1% and 22.4%, respectively. © TÜBİTAK.
  • Article
    Citation - WoS: 19
    Citation - Scopus: 22
    Optimization 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 Şebnem
    The 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.
  • Master Thesis
    Transformation of Aspergillus Sojae With Vitreoscilla Hemoglobin Gene
    (Izmir Institute of Technology, 2010) Bardakçı, Betül; Tarı, Canan; Tari, Canan
    Aspergillus sojae known as koji mold is a non-aflatoxigenic fungus, designated with a GRAS status by FDA. This study considers the transformation of A. sojae with Vitreoscilla hemoglobin gene. Vitreoscilla hemoglobin is the bacterial hemoglobin, which enhances the oxygen transfer under microaerophilic conditions. Since industrial fungal fermentation with the high demand for oxygen are accounted to face oxygen limitations during the production of value added products like enzymes, antibiotics and organic acids; oxygen supply becomes an enormous problem to be solved by the manufacturers. To overcome this problem, an alternative solution using the vgb gene of Vitreoscilla and recombinant DNA technology and taking the A. sojae organism as model organism was proposed. The product of interest in this study was the exopolygalacturonase enzyme known to have wide applications in food, pharmaceutical, textile and paper industries. Here vgb gene was tried to be introduced to A .sojae via both protoplasting and electroporation methods. For transformation process vgb gene was cloned initially into plasmid ANIp4. For the selection of transformed A. sojae cells, uridine auxotrophic mutants were tried to be selected after UV mutagenesis. However, using a procedure based on selection of uridine supported growth did not result in A. sojae pyrG mutants. The success of transformation was initially observed by means of PCR analysis and agarose gel electrophoresis, later this was try to be confirmed by sequence analysis and agarose gel electrophoresis. However, due to the contamination problems accounted in the procedures the transformation with both methods could not be assured.
  • Article
    Citation - WoS: 110
    Citation - Scopus: 120
    Alkaline Protease Production From Alkalophilic Bacillus Sp. Isolated From Natural Habitats
    (Elsevier Ltd., 2006) Gençkal, Hande; Tarı, Canan
    Bacillus strains isolated under extreme alkaline conditions (Izmir, Turkey), were screened and identified for high alkaline protease activity. Strains with high protease yields were optimized with respect to inoculum concentration, temperature, agitation speed, initial medium pH and incubation time. Three Bacillus strains coded as I18, L18 and L21 showed high potential, for alkaline protease activity (160-222 U/ml) among 85 isolates. The specific growth rates were estimated from the growth curves as 0.49 h-1 for I18, as 0.6 and 0.7 h-1 for L18 and L21, respectively. The optimum temperatures were determined as 30 °C for strain I18 and 37 °C for the strains L18 and L21. Similarly, the optimum agitation speeds were 100 rpm for I18 and 180 rpm for L18 and L21. For all three strains, the optimum inoculation ratio and incubation time, were determined as 5% (v/v) and 96 h, respectively. The optimum initial media pH was found as pH 10 for strain L18 and L21. Bacillus sp. L21 with the highest specific protease activity (60 U/mg protein) and a broader pH range was chosen for further study. The biomass and product yield for this strain was determined as 0.023 g cell/g glucose and 0.021 U/g glucose, respectively. The crude enzyme of this strain was further characterized and was determined as a bleach stable, serine alkaline protease with an optimum temperature of 60 °C and a pH of 11, with a potential to be a candidate for the applications in the detergent industry.