eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
87
93
7159
Statistical optimization of arachidonic acid production by Mortierella alpina CBS 754.68 in submerged fermentation
Karim Rocky-Salimi
1
Zohreh Hamidi-Esfahani
hamidy_z@modares.ac.ir
2
Soleiman Abbasi
3
Department of Food Science and Technology, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115- 336, Tehran, I.R. Iran.
Department of Food Science and Technology, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115- 336, Tehran, I.R. Iran.
Department of Food Science and Technology, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115- 336, Tehran, I.R. Iran.
Arachidonic acid is an essential fatty acid in human nutrition. In the present study, production of arachidonicacid by Mortierella alpina CBS 754.68 was evaluated in submerged fermentation. The fermentation variableswere selected in accordance with the Plackett-Burman (PB) design and further optimized via response surface methodology (RSM). Five significant variables, namely glucose, yeast extract, temperature,agitation rate, and fermentation time were selected for the optimization studies. The statistical model was constructed via central composite design (CCD). Following the optimization step arachidonic acid production increased by approximately 660.5%, when compared to the screening step. The results indicate that carrying out the fermentation under the conditions of glucose at 50 g/l; yeast extract at 14 g/l; temperature of 22°C; agitation rate of 180 rpm, and fermentation time of 8 days will increase the arachidonic acid production up to 3 g/l. Results show that the optimization of culture conditions could greatly increase arachidonic acid production by Mortierella alpina CBS 754.68.
https://www.ijbiotech.com/article_7159_f056368cccb3a6a9b64347d8f2140aa2.pdf
Arachidonic acid
Mortierella alpina
Plackett-Burman (PB) design
Response surface methodology (RSM)
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
94
101
7160
Biotechnological production of cellulose by Gluconacetobacter xylinus from agricultural waste
Marzieh Moosavi-Nasab
1
Alireza Yousefi
2
Department of Food Science and Technology, University of Shiraz, P.O. Box 7144165186, Shiraz, I.R. Iran.
Department of Food Science and Technology, University of Shiraz, P.O. Box 7144165186, Shiraz, I.R. Iran.
The purpose of this study was to utilize low quality date syrup, a rich and available source of nutrient in Iran, for the production of bacterial cellulose using Gluconacetobacter xylinus. Static batch fermentationfor the purpose of cellulose production by G. xylinus (PTCC, 1734) was studied using low quality date syrupand sucrose solution (Bx. 10%) as fermentation media at 28°C. Results showed that maximum yields of bacterial cellulose after 336 h fermentation were 4.35 and 1.69 g/100 ml of date syrup and sucrose media,respectively. The FT-IR spectrum of commercial plant cellulose as a standard was similar to that of bacterialcellulose. To determine the physical structure of the bacterial cellulose and standard cellulose fibers, scanningelectron microscopy (SEM) was carried out. The results revealed more delicacy in structure of bacterialcellulose. Determination of crystallinity of the samples using X-ray diffractometry demonstrated that the crystallinity level of standard cellulose (83.61%) was more than that of bacterial cellulose (60.73%). This studyobviously showed the ability of low quality date syrup, a suitable and cheap carbon source, to be used as asubstrate in a fermentation medium for production of cellulose by Gluconacetobacter xylinus.
https://www.ijbiotech.com/article_7160_0b08b73a1b4dce00a4415f3abebb65e6.pdf
Cellulose
Date syrup
G. xylinus
Fourier transform infrared spectroscopy
Scanning electron microscopy
X-ray diffractometry
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
102
108
7161
Study of L-asparaginase production by Streptomyces noursei MTCC 10469, isolated from marine sponge Callyspongia diffusa
Selvakumar Dharmaraj
biochem_selva@yahoo.com
1
Department of Aquatic Biology and Fisheries, University of Kerala, Kariavattom campus, Trivandrum 695 581, Kerala, India.
L-asparaginase is an anti-neoplastic agent used in the chemotherapy of lymphoblastic leukaemia. The present work deals with production of extra-cellular Lasparaginase from marine actinomycetes, using submerged fermentation. Marine actinomycete Streptomyces associated with marine spongeCallyspongia diffusa was isolated using specific ISP medium. Sponge-associated Streptomyces was characterized by conventional methods, and identified as Streptomyces noursei MTCC 10469. Production of Lasparaginase by submerged fermentation was carried out using medium Tryptone Glucose Yeast extract(TGY) broth. The enzyme was purified to near homogeneity by ammonium sulphate precipitation, dialysis,gel filtration on Sephadex G-100 column, CM Sephadex C-50 and SDS-PAGE. The enzyme was purified at 98.23 folds, and showed a final specific activity of 78.88 IU/mg, with 2.14% yield. SDS-PAGE of the purified enzyme revealed an apparent molecular weight of 102 kDa for it. The optimum pH, temperature and incubation time of L-asparaginase was found to be 8, 50ºC and 35 min, respectively. The study suggeststhat marine actinomycetes, particularly Streptomyces, may be used as a potential source of L-asparaginase.
https://www.ijbiotech.com/article_7161_45fe59829bacb2fcc84f42ba435c3be8.pdf
Marine actinomycetes
Streptomyces
Lasparaginase
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
109
114
7127
Characterization of an interesting novel mutant strain of commercial Saccharomyces cerevisiae
Mohsen Mobini-Dehkordi
mmobinid@gmail.com
1
Iraj Nahvi
i.nahvi@sci.ui.ac.ir
2
Hamid Zarkesh-Esfahani
3
Kamran Ghaedi
kamranghaedi@sci.ui.ac.ir
4
Manoochehr Tavassoli
manoochehr@sci.ui.ac.ir
5
Rinji Akada
6
Department of Genetics, Faculty of Sciences, University of Shahrekord, P.O. Box 115, Shahrekord, I.R. Iran.
Department of Biology, Faculty of Sceinces, University of Isfahan, P.O. Box 81745-141, Isfahan, I.R. Iran.
Department of Biology, Faculty of Sceinces, University of Isfahan, P.O. Box 81745-141, Isfahan, I.R. Iran.
Department of Biology, Faculty of Sceinces, University of Isfahan, P.O. Box 81745-141, Isfahan, I.R. Iran.
Department of Biology, Faculty of Sceinces, University of Isfahan, P.O. Box 81745-141, Isfahan, I.R. Iran.
Department of Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Tokiwadai, Ube 755-8611, P.O. Box 8611-755, Japan.
The yeast strains that are resistant to high concentration of ethanol have biotechnological benefits and aresuitable models for physiology and molecular genetics research fields. A novel ethanol-tolerant mutant strain,mut1, derived from the commercial Saccharomyces cerevisiae showed higher ethanol production, and alsodemonstrated resistance to ethanol but not to other alcohols, such as methanol, 2-propanol, and 1-butanol. To characterize mut1, the strain’s resistance to other organic compounds and osmotic and cell wallstresses were examined. The growth of the mut1 strain in the presence of ethyl n-caproate and 3-methyl butylacetate, which were metabolic derivatives of ethanol, was found to be less than the wild type. On the otherhand, the growth of the mut1 strain in the presence of 50% (w/v) sucrose and 1M NaCl was similar to that ofthe wild type. The sensitivity to cell wall digestive enzyme, zymolyase, was also similar in both wild andmut1 strains. Finally, the mut1 strain showed resistance to homocysteine and serine but was sensitive tomethionine. These results suggest that the ethanol resistance of the mut1 strain may be more related tothe ethanol metabolic and signalling pathways rather than the enhanced stress resistances relating to themembrane or cell wall compositions.
https://www.ijbiotech.com/article_7127_e98675d8b1be2196f3b5d604dc1ac50f.pdf
Ethanol
tolerance
Metabolic and signalling pathways
Fermentation
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
115
119
7130
Polymorphism of Prion Protein Gene (PRNP) in Iranian Holstein and two local cattle populations (Golpayegani and Sistani) of Iran
Saber Mohammad Maghsoodi
1
Seyed Reza Miraei-Ashtiani
2
Mohammad Hossein Banabazi
hossein.banabazi@gmail.com
3
Hassan Mehrabani Yeganeh
4
Department of Animal Science, University College of Agriculture and Natural Resources, University of Tehran, Karaj, P.O. Box 4111, I.R. Iran.
Department of Animal Science, University College of Agriculture and Natural Resources, University of Tehran, Karaj, P.O. Box 4111, I.R. Iran.
Department of Biotechnology, Animal Science Research Institute of Iran, Karaj, P.O. Box 1483, I.R. Iran.
Department of Animal Science, University College of Agriculture and Natural Resources, University of Tehran, Karaj, P.O. Box 4111, I.R. Iran.
Bovine spongiform encephalopathy (BSE) is a fatal infectious neurodegenerative disease in cattle, characterized by the accumulation of an abnormal, proteaseresistant prion protein (PrPSc) in the brain. BSE is similar to scrapie in sheep and goats and Creuzfeldt-Jakob disease in humans. Susceptibility in cattle hasbeen shown to be under the influence of two polymorphic locations, which are a 23 bp in/del polymorphismand a 12 bp indel within intron 1 of the prion protein gene (PRNP). DNA was extracted from blood samplesof three Iranian cattle populations including Sistani (Bos indicus) (n=60), Golpayegani (Bos indicus) (n=62) and Iranian Holstein (Bos taurus) (n=50), In order to identify the putative polymorphisms of the PRNP gene of those breeds. Allele, genotype and haplotype frequencies of the polymorphisms were determined for the three populations. Susceptibility analysis was considered as per literature, upon which, it was suggested that the two Bos indicus native populations are more resistant to BSE than the Iranian Holstein (Bos taurus), due to higher gene frequency for insertion allele of the intron 1 of the PRNP gene polymorphism.
https://www.ijbiotech.com/article_7130_bc4a986c5089fce8f8411799e346690a.pdf
Bovine Spongiform Encephalopathy (BSE)
PRNP gene
Iranian Holstein
Golpayegani cattle
Sistani cattle
Genetic susceptibility
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
120
125
7133
Molecular diversity of mitochondrial DNA in Iranian Azeri ethnicities vis-à-vis other Azeris in Asia
Mohammad Asgharzadeh
1
Hossein Samadi Kafil
2
Ahmad Ranjbar
3
Ali Rahimipour
4
Kazem Najati
5
Mohammad Rahbani Nobar
6
Biotechnology Research Center, Tabriz University of Medical Sciences, P.O. Box 51666-14766, Tabriz, I.R. Iran.
Epidemiology Research Center, Aja University of Medical Sciences, P.O. Box 1411718541, Tehran, I.R. Iran.
Hematology and Oncology Research Center, Tabriz Univeristy of Medical Sciences, P.O. Box 51666-14766, Tabriz, I.R. Iran.
Department of Clinical Biochemistry, Shahid Beheshti University of Medical Sciences, P.O.Box: 1985717443, Tehran, I.R. Iran.
Biotechnology Research Center, Tabriz University of Medical Sciences, P.O. Box 51666-14766, Tabriz, I.R. Iran.
Biotechnology Research Center, Tabriz University of Medical Sciences, P.O. Box 51666-14766, Tabriz, I.R. Iran.
In order to investigate the molecular diversity of mtDNA in Azeri population, 133 Azeri subjects inhabitingdifferent regions of Azerbaijan (Iran) were selected. Blood samples were taken from these subjects formtDNA extraction. The extracted mtDNA samples were then studied by the PCR-RFLP method.Fourteen haplogroups were characterized from which 82% were identified as European specific haplogroups.The H haplogroup was the most frequent and 79 haplotypes were specified. In this study, the Iranian Azeri population was found to be a heterogenic population where all the specific haplogroups of Asians, Europeans and Africans were present in the studied population. Comparing the haplogroups of the present investigation with other populations indicated a very close similarity with other Iranian populations, but was different from haplogroups of other Asian populations who also speak the Azeri language.
https://www.ijbiotech.com/article_7133_52742d9b84b8766f08e95ebf73f73f0c.pdf
Azeri
population
Iran
MtDNA
Diversity
Haplogroup
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
126
132
7131
Heme oxygenase-2 gene mutations and blood bilirubin level in Iranian patients with premature atherosclerosis
Ahmad Aleyasin
sogand@nigeb.ac.ir
1
Mohammad Zamani
2
Hossien Fakhrzadeh
3
Majid Kiavar
4
Somaieh Raoufzadeh
5
Bagher Larijani
6
Ebrahim Mahmodi
7
National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran.
National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran.
Endocrine and Metabolism Research Center, Tehran University of Medical Sciences and Health Services, P.O. Box 14155-1771, Tehran, I.R. Iran.
Shaheed Rajaei Cardiovascular Medical and Research Center, P.O. Box 1996911151, Tehran, I.R. Iran.
National Institute of Genetic Engineering and Biotechnology, P.O. Box 14965/161, Tehran, I.R. Iran.
Endocrine and Metabolism Research Center, Tehran University of Medical Sciences and Health Services, P.O. Box 14155-1771, Tehran, I.R. Iran.
Shaheed Rajaei Cardiovascular Medical and Research Center, P.O. Box 1996911151, Tehran, I.R. Iran.
Heme oxygenase-2 (HO-2) is a critical antioxidative stress enzyme found in endothelial cells and adventitialnerves. This enzyme in conjunction with other HOs (1 and 3) metabolize heme molecule into ferrous iron,carbon monoxide (CO), and biliverdin which is further converted to bilirubin. Both biliverdin and bilirubin arepotent antioxidants, reducing the risk of atherosclerosis. HO-2 also induces endothelial relaxation by synthesizing CO. This is the first study to evaluate the association of HO-2 gene mutation in patients affectedwith atherosclerosis. Blood samples from patients (n=137) and normal controls (n=100) were collected.Three pairs of primers were designed to amplify exons 2 to 4 related to human HO-2 gene. The PCR productswere analyzed by SSCP and sequencing to find out mutations. Iron and bilirubins (Total, Direct andIndirect) levels were determined in patients and controls. Two nucleotide substitutions were found among10% of patients, consisted of a newly reported transversion mutation, C to A substitution in codon A70D(GCC to GAC) (Ala to Asp) and a previously reported transition mutation, A to G substitution in codon K89E(AAG to GAG) (Leu to Glu). Significant associations were obtained between risk of atherosclerosis andA437G substitution in codon K89E of HO-2 gene (P6.82) and reduced level of total (P6.01), and indirect (P< 0.016 and χ2>5.99) bilirubins with no significant association with serum iron and direct bilirubin. No significant associations were observed among C381A substitution incodon (A70D, P< 0.11 and χ2 >2.97), level of serum iron, bilirubin and risk of atherosclerosis. These findings indicate the importance of A437G substitution in the development of atherosclerosis. Further studies are required to study the association of HO-2 gene mutations with atherosclerosis in other populations.
https://www.ijbiotech.com/article_7131_0b2a03fb405871446dca5437f588f378.pdf
Atherosclerosis
Heme oxygenase-2
bilirubin
CAD
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
133
144
7134
A study of Acidithiobacillus ferrooxidans DSMZ 583 adaptation to heavy metals
Sima Molaei
1
Soheila Yaghmaei
yaghmaei@sharif.edu
2
Zahra Ghobadi
3
Department of Chemical and Petroleum Engineering, Sharif University of Technology, P.O. Box 11155-9465, Tehran, I.R. Iran.
Department of Chemical and Petroleum Engineering, Sharif University of Technology, P.O. Box 11155-9465, Tehran, I.R. Iran.
Biochemical and Bioenvironmental Research Center, Sharif University of Technology, P.O. Box: 11155-1399, Tehran, I.R. Iran.
In this study the ability of Acidithiobacillus ferrooxidans, with regard to the biorecovery of heavy metals inshake flask has been investigated. Adaptation experiments with the single metal ions Ni, Co, V, Mo, W anda mixture of the first four metal ions in the medium was developed through serial sub-culturing. Adaptationshowed that A. ferrooxidans could tolerate up to 2.3 g/l Ni, 1.4 g/l Co, 1.4 g/l V, 0.045 g/l Mo and 0.005 g/l W, singly. In the presence of multi-metals considering a mixture of Ni-Co-V-Mo, the bacteria was able to tolerate up to 1.5 g/l Ni, 0.8 g/l Co, 0.8 g/l V and 0.05 g/l Mo in steps of 50-100 mg/l for Ni, Co and V, while for Mo and W with increments in concentration of 1-5 ppm, because of the high toxicity of these two metals to the bacteria. Adaptation of the bacterial strain was carried out in batch cultures by continually growing the bacteria in an environment containing increasing concentrations of the toxic metal such that a culture tolerant to the toxic metal proliferates. Effects of several variables such as pH, Eh, bacterial concentration in the solution as well as its resistance to heavy metals and ferrous and ferric iron concentration for the specific bacterial growth rate, were also investigated. This study showed that the various concentrations of Ni, Co and V had little effect on the oxidation of ferrous iron or the cell growth of A. ferrooxidans, whereas Mo and W ionswere very inhibitory towards the Fe+2 oxidation ability of A. ferrooxidans.
https://www.ijbiotech.com/article_7134_9348cacfad940b61debdf117a6b42657.pdf
Acidithiobacillus ferrooxidans
adaptation
Biorecovery
heavy metals
eng
National Institute of Genetic Engineering and Biotechnology of Iran
Iranian Journal of Biotechnology
1728-3043
2322-2921
2011-04-01
9
2
145
149
7135
Characterization of calpastatin gene in Iranian Afshari sheep
Navid Dinparast Djadid
navidmvrg2@gmail.com
1
Mehdi Nikmard
2
Sedigheh Zakeri
3
Saber Gholizadeh
4
Malaria and Vector Research Group, Biotechnology Research Center, Pasteur Institute of Iran, P.O. Box:1316943551, Tehran, I.R. Iran.
Animal Science Department, College of Agriculture, University of Zanjan, P.O. Box 313, Zanjan, I.R. Iran.
Malaria and Vector Research Group, Biotechnology Research Center, Pasteur Institute of Iran, P.O. Box:1316943551, Tehran, I.R. Iran.
Malaria and Vector Research Group, Biotechnology Research Center, Pasteur Institute of Iran, P.O. Box:1316943551, Tehran, I.R. Iran.
Calpastatin is an endogenous inhibitor of calpain (calcium-dependent cysteine protease). Calpastatin activityis highly related to the rate of protein turnover and rate of meat tenderization. In order to characterize thestructure of calpastatin in Iranian Afshari breed of sheep, intron 6 and partial exon 7 of the L domain wereamplified and sequenced. A fragment of approximately 1.5 kb was identified. In this study, an Afshari calpastatin gene fragment that encoded L Domain amino acids was detected. Hence by detection of such conserved mutations, it is possible to use these polymorphisms in Marker-Assisted Selection (MAS).
https://www.ijbiotech.com/article_7135_776e71d4ef0f4d80c9b8e009df5c5d84.pdf
Calpastatin
Sequence analysis
Iran
Afshari sheep