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ABSTRACT: Corn seed is a major ingredient of animal feed worldwide. However, it contains phytate, a major phosphate storage form that is unavailable to monogastric animals like pigs and poultry. We report a transgenic corn with bioavailable phosphate, achieved by seed-specific overexpression of Aspergillus niger phytase, an enzyme catalyzing the release of phosphate from phytate. We obtained maximal phytase activity of 125 FTU/g kernels, 1000-fold above that of the wild type, with 1000 g of kernels containing up to 67 times the feed industry requirement. Enzymatic characterization of Zea mays recombinant phytase (ZmrPhy) showed it to be equivalent to yeast (Pichia pastoris) recombinant phytase (PprPhy), a commercially available phytase product. An animal feeding trial demonstrated that ZmrPhy had similar nutritional effects on broiler chickens to PprPhy in terms of reducing inorganic phosphorus addition to feed and phosphate excretion in animal manure. These results suggest that transgenic phytase corn can be used directly in the feed industry. Experiments were conducted to assess the food safety of the corn; the results demonstrated no difference versus regular corn. This is the first genetically modified corn officially issued with a biosafety certificate in China and has great potential in the animal feed industry.
Journal of biotechnology 03/2013; · 2.88 Impact Factor
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ABSTRACT: We cloned a Paenibacillus sp. E18 5.3-kb xylanolytic gene cluster that contains three open reading frames encoding two family-43 α-l-arabinofuranosidases (Abf43A and Abf43B) and one family-10 xylanase (XynBE18). The deduced amino acid sequences of Abf43A and Abf43B were at most 68% and 63% identical with two putative family-43 proteins from Clostridium sp. DL-VIII (EHI98634.1 and EHI98635.1), respectively, but were only 11% identical with each other. Recombinant Abf43A and Abf43B had similar activities at 45°C and pH 6.0, but varied in thermostabilities and substrate specificities. Abf43B was active against only 4-nitrophenyl α-l-arabinofuranoside, whereas Abf43A acted on 4-nitrophenyl α-l-arabinofuranoside, wheat arabinoxylan, 4-nitrophenyl α-d-xylopyranoside, and sugar beet arabinan. The sequential and combined effects on xylan degradation by XynBE18, Abf43A, and Abf43B were characterized. For beechwood, birchwood, and oat spelt xylans as substrates, synergistic effects were found when XynBE18 and Abf43A or Abf43B were incubated together and when the substrates were first incubated with Abf43A or Abf43B and then with XynBE18. Further HPLC analysis showed that the amounts of xylobiose and xylose increased sharply in the aforementioned reactions. For water-soluble wheat arabinoxylan as substrate, Abf43A not only released arabinose but also had synergistic effect with XynBE18. Synergy may arise as the result of removal of arabinose residues from xylans by α-l-arabinofuranosidases, which eliminates steric hindrance caused by the arabinose side chains and which allows xylanases to then degrade the xylan backbone, producing short xylooligosaccharides.
Applied and environmental microbiology 01/2013; · 3.69 Impact Factor
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ABSTRACT: A novel β-mannanase gene, man5XZ7, was cloned from thermophilic fungus Thielavia arenaria XZ7, and successfully expressed in Pichia pastoris. The gene (1,110 bp) encodes a 369-amino acid polypeptide with a molecular mass of approximately 40.8 kDa. The deduced sequence of Man5XZ7 consists of a putative 17-residue signal peptide and a catalytic module belonging to glycoside hydrolase (GH) family 5, and displays 76 % identity with the experimentally verified GH 5 endo-β-1,4-mannanase from Podospora anserina. Recombinant Man5XZ7 was optimally active at 75 °C and pH 5.0 and exhibited high activity at a wide temperature range (>50.0 % activity at 50-85 °C). Moreover, it had good adaptability to acidic to basic pH (>74.1 % activity at pH 4.0-7.0 and 25.6 % even at pH 9.0) and good stability from pH 3.0 to 10.0. These enzymatic properties showed that Man5XZ7 was a new thermophilic and alkali-tolerant β-mannanase. Further amino acid composition analysis indicated that Man5XZ7 has several characteristic features of thermophilic enzymes.
Applied Microbiology and Biotechnology 01/2013; · 3.42 Impact Factor
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ABSTRACT: A novel β-glucosidase gene, bgl1G5, was cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. Sequence analysis indicated that the gene consists of a 1,431-bp open reading frame encoding a protein of 476 amino acids. The deduced amino acid sequence of bgl1G5 showed a high identity of 85 % with a characterized β-glucosidase from Humicola grisea of glycoside hydrolase family 1. Compared with other fungal counterparts, Bgl1G5 showed similar optimal activity at pH 6.0 and 50 °C and was stable at pH 5.0-9.0. Moreover, Bgl1G5 exhibited good thermostability at 50 °C (6 h half-life) and higher specific activity (54.9 U mg(-1)). The K (m) and V (max) values towards p-nitrophenyl β-D-glucopyranoside (pNPG) were 0.33 mM and 103.1 μmol min(-1) mg(-1), respectively. The substrate specificity assay showed that Bgl1G5 was highly active against pNPG, weak on p-nitrophenyl β-D-cellobioside (pNPC) and p-nitrophenyl-β-D-galactopyranoside (ONPG), and had no activity on cellobiose. This result indicated Bgl1G5 was a typical aryl β-glucosidase.
Applied biochemistry and biotechnology 01/2013; · 1.94 Impact Factor
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ABSTRACT: Mannans and heteromannans are widespread in plants cell walls and are well-known as anti-nutritional factors in animal feed. To remove these factors, it is common practice to incorporate endo-β-mannanase into feed for efficient nutrition absorption. The objective of this study was to overexpress a β-mannanase gene directly in maize, the main ingredient of animal feed, to simplify the process of feed production.
The man5A gene encoding an excellent β-mannanase from acidophilic Bispora sp. MEY-1 was selected for heterologous overexpression. Expression of the modified gene (man5As) was driven by the embryo-specific promoter ZM-leg1A, and the transgene was transferred to three generations by backcrossing with commercial inbred Zheng58. Its exogenous integration into the maize embryonic genome and tissue specific expression in seeds were confirmed by PCR and Southern blot and Western blot analysis, respectively. Transgenic plants at BC3 generation showed agronomic traits statistically similar to Zheng58 except for less plant height (154.0 cm vs 158.3 cm). The expression level of MAN5AS reached up to 26,860 units per kilogram of maize seeds. Compared with its counterpart produced in Pichia pastoris, seed-derived MAN5AS had higher temperature optimum (90°C), and remained more β-mannanase activities after pelleting at 80°C, 100°C or 120°C.
This study shows the genetically stable overexpression of a fungal β-mannanase in maize and offers an effective and economic approach for transgene containment in maize for direct utilization without any purification or supplementation procedures.
PLoS ONE 01/2013; 8(2):e56146. · 4.09 Impact Factor
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ABSTRACT: Three xylanase genes (xynA, xynB, xynC) of glycosyl hydrolase family 10 were identified in Humicola insolens Y1. The deduced protein sequences showed the highest identity of ⩽83% to known fungal xylanases and of ⩽38% with each other. Recombinant XynA-C produced in Pichia pastoris showed optimal activities at pH 6.0-7.0 and at high temperature (70-80°C), and exhibited good stability over a broad pH range and temperatures at 60°C. The gene xynC produced by H. insolens Y1 (named XynW) was similar in enzyme properties with XynC expressed by Pichia. XynA exhibited better alkaline adaptation and thermostability, and had higher catalytic efficiency and wider substrate specificity. Under simulated mashing conditions, addition of XynA-C showed better performance on filtration acceleration (37.4%) and viscosity reduction (13.5%) than Ultraflo from Novozyme. Thus the three xylanases represent good candidates for application in the brewing industry.
Bioresource technology 12/2012; 130C:161-167. · 4.25 Impact Factor
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ABSTRACT: Xylanase is a crucial hydrolytic enzyme that degrades plant polysaccharides in the rumen. To date there is no information on the genetic composition and expression characteristics of ruminal xylanase during feeding cycles of ruminants. Here, the major xylanase of the glycoside hydrolase family 10 from the rumen of Small Tail Han sheep was investigated during a feeding cycle. We identified 44 distinct GH 10 xylanase gene fragments at both genomic and transcriptional levels. Comparison of their relative abundance showed that evaluating functional genes at the transcription level is a more reliable indicator for understanding fluctuations in xylanase levels. The expression patterns of six xylanase genes, detected at all time points of the feeding cycle, were investigated; we observed a complex trend of gene expression over 24 h, revealing the dynamic expression of xylanases in the rumen. Further correlation analysis indicates that the rumen is a dynamic ecosystem where the transcript profiles of xylanase genes are closely related to ruminal conditions, especially rumen pH and bacterial population. Given the huge diversity and changing composition of enzymes over the entire rumen, this research provides valuable information for understanding the role of functional genes in the digestion of plant material.
Applied and environmental microbiology 12/2012; · 3.69 Impact Factor
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ABSTRACT: A xylanase gene, xyn-b39, coding for a multidomain glycoside hydrolase (GH) family 10 protein was cloned from the genomic DNA of the alkaline wastewater sludge of a paper mill. Its deduced amino acid sequence of 1,481 residues included two carbohydrate-binding modules (CBM) of family CBM_4_9, one catalytic domain of GH 10, one family 9 CBM and three S-layer homology (SLH) domains. xyn-b39 was expressed heterologously in Escherichia coli, and the recombinant enzyme was purified and characterized. Xyn-b39 exhibited maximum activity at pH 7.0 and 60 °C, and remained highly active under alkaline conditions (more than 80 % activity at pH 9.0 and 40 % activity at pH 10.0). The enzyme was thermostable at 55 °C, retaining more than 90 % of the initial activity after 2 h pre-incubation. Xyn-b39 had wide substrate specificity and hydrolyzed soluble substrates (birchwood xylan, beechwood xylan, oat spelt xylan, wheat arabinoxylan) and insoluble substrates (oat spelt xylan and wheat arabinoxylan). Hydrolysis product analysis indicated that Xyn-b39 was an endo-type xylanase. The K (m) and V (max) values of Xyn-b39 for birchwood xylan were 1.01 mg/mL and 73.53 U/min/mg, respectively. At the charge of 10 U/g reed pulp for 1 h, Xyn-b39 significantly reduced the Kappa number (P < 0.05) with low consumption of chlorine dioxide alone.
MIRCEN Journal of Applied Microbiology and Biotechnology 11/2012; · 1.08 Impact Factor
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ABSTRACT: Alkaline pectate lyases are favorable for the textile industry. Here, we report the gene cloning and expression of a low-temperature-active alkaline pectate lyase (PL D) from Xanthomonas campestris ACCC 10048. Deduced PL D consists of a putative 27-residue signal peptide and a catalytic domain of 320 residues belonging to family PF09492. Recombinant PL D (r-PL D) produced in Escherichia coli was purified to electrophoretic homogeneity with a single step of Ni(2+)-NTA affinity chromatography and showed an apparent molecular weight of ~38 kDa. The pH and temperature optima of r-PL D were found to be 9.0 °C and 30 °C, respectively. Compared with its microbial counterparts, r-PL D had higher activity over a wide pH range (>45 % of the maximum activity at pH 3.0-12.0) and at lower temperatures (>35 % of activity even at 0 °C). The K (m) and V (max) values of r-PL D for polygalacturonic acid were 4.9 g l(-1) and 30.1 μmol min(-1) mg(-1), respectively. Compared with the commercial compound pectinase from Novozymes, r-PL D showed similar efficacy in reducing the intrinsic viscosity of polygalacturonic acid (35.1 % vs. 36.5 %) and in bioscouring of jute (10.25 % vs. 10.82 %). Thus, r-PL D is a valuable additive candidate for the textile industry.
Applied biochemistry and biotechnology 09/2012; · 1.94 Impact Factor
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ABSTRACT: Trimethoprim/sulfamethoxazole is widely used in the treatment of infectious diseases caused by bacterial pathogens in aquaculture. However, the practice of antibiotic administration can promote the emergence of resistant strains of bacteria and result in a wane in efficacy over time. The objective of this study was to assess the effect of oral treatment with trimethoprim/sulfamethoxazole on the gastrointestinal (GI) microbiota of healthy gibel carp and those affected with bacterial enteritis. By using denaturing gradient gel electrophoresis (DGGE), the changes in the predominant bacterial communities were directly depicted for the first time. The main findings were (1) Actinobacteria, Firmicutes and Proteobacteria were the predominant phyla in the healthy gibel carp intestine; (2) administration of antibiotics had a more profound impact on the intestinal microflora of healthy fish than of the diseased ones; and (3) Enterobacteriaceae might be one of the major drug-resistant bacteria in the gibel carp intestine. This study provides an insight into the effect of antibiotic treatment on the establishment and colonization of fish GI microbiota and speculates on some possible drug-resistant bacteria.
Diseases of Aquatic Organisms 07/2012; 99(3):207-13. · 2.20 Impact Factor
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ABSTRACT: Polygalacturonases are important feed and food additives. In the present study an exo-polygalacturonase gene (pgu B) was cloned from Klebsiella sp. Y1 CGMCC 4433 and expressed in Escherichia coli BL21 (DE3). pgu B encodes a 658-amino acid polypeptide belonging to Glycoside Hydrolase Family 28. The optimal pH and temperature of exo-PGU B activity were 6.0 and 40-50°C, respectively. The enzyme exhibited >35% of maximum activity within the pH range of 2.0-12.0. Exo-PGU B or an exo-PGU B/ endo-polygalacturonase mixture reduced the viscosity of polygalacturonic acid (1.0%, w/v) by 15.6 and 39.4%, respectively. Under simulated alimentary tract conditions, exo-PGU B was very stable (>25% activity from pH 1.5 to 6.8) and active, releasing 53.7 and 109.6μg of galacturonic acid from 400 to 800μg of polygalacturonic acid, respectively. These properties make exo-PGU B a potentially valuable additive for applications in feed and food.
Bioresource technology 07/2012; 123:171-6. · 4.25 Impact Factor
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ABSTRACT: Two novel cellulase genes, cbh6A and egGH45, were cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. The putative polypeptide of CBH6A consists of a family 1 CBM and a catalytic domain of glycosyl hydrolase family 6 cellobiohydrolases, while deduced EgGH45 only contains a catalytic domain of family 45 endoglucanases. CBH6A and EgGH45 were optimally active at pH 7.0 and 65°C, and pH 6.0 and 60°C, respectively. Both enzymes exhibited high activities and stabilities over a wide pH range and had good thermostability at 70°C. CBH6A and EgGH45 had significant resistance to SDS (10mM), remaining 35% and 54% activities, respectively. These enzymes had synergic effect on the hydrolysis of filter paper, showing the highest efficiency in the ratio of CBH6A to EgGH45 at 80:20. The properties make this enzyme combination potential for application in textile and detergents industries.
Bioresource technology 07/2012; 121:404-10. · 4.25 Impact Factor
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ABSTRACT: An extracellular β-1,4-glucanase (CelG5, ∼55.0kDa) was isolated from the culture filtrate of Phialophora sp. G5, and its encoding gene was cloned. The deduced amino acid sequence of CelG5 was at most 73.6% and 44.0%, respectively, identical with a hypothetical protein from Sordaria macrospora and an experimentally verified GH 7 endo-β-1,4-glucanase of Neurospora tetrasperma FGSC 2508. Native CelG5 had pH and temperature optima of pH 4.5-5.0 and 55-60°C. The enzyme showed some properties superior than most fungal β-1,4-glucanases, such as high activity over a wide pH range (exhibiting >50% of the maximum activity at pH 2.0-7.0), excellent stability in extreme acidic to alkaline conditions (pH 2.0-9.0), and strong resistance against pepsin and trypsin (retaining 89% and 94% activity, respectively). Recombinant CelG5 produced in Pichia pastoris had a molecular mass and a pH optimum similar to native CelG5, but with maximal activity at 65°C. Application tests showed that native CelG5 was stable under simulated gastric conditions (retaining >70% activity), and had capacity to decrease the viscosity of barley-bean feed (8.9% by 200U CelG5) and mash (6.1% by 50U CelG5) and increase the filtration rate of mash (18.4% by 50U CelG5). These properties make CelG5 a good candidate for utilization in the animal feed and brewing industries.
Journal of Bioscience and Bioengineering 05/2012; 114(4):379-84. · 1.79 Impact Factor
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ABSTRACT: Using degenerate polymerase chain reaction (PCR), thermal asymmetric interlaced (TAIL)-PCR, and reverse transcription (RT)-PCR
techniques, a new β-mannanase gene, denoted as man5C6, was obtained from Penicillium sp. C6. The gene has an open reading frame of 1,155bp, and codes for a polypeptide (Man5C6) of 384 amino acids including
a putative 26-residue signal peptide. The deduced amino acid sequence showed highest identity (59.2%) with an experimentally
verified β-mannanase from Podospora anserine belonging to glycoside hydrolase family 5. Man5C6 was successfully expressed in Pichia pastoris, and secreted up to 2.5g in 1l medium. Recombinant Man5C6 was easily purified to electrophoretic homogeneity by a sing-step
chromatography. The purified recombinant enzyme exhibited optimal activity at pH 4.5, and remained>55% of its maximum activity
at pH 3.0–7.0. The temperature optimum was found to be 70°C. The specific activity, and K
m and V
max values were 226.5 U mg−1, 12.3mgml−1 and 2,400.2μmolmin−1 mg−1, respectively, for locust bean gum, and 78.7Umg−1, 0.2mgml−1 and 894.6μmolmin−1 mg−1, respectively, for konjac flour. These properties make Man5C6 a potential candidate for high-level production of β-mannanase
with low cost and simple processing technology.
Keywords
Penicillium sp. C6–β-Mannanase–
Pichia pastoris
–Over-expression
World Journal of Microbiology and Biotechnology 05/2012; 27(12):2813-2819. · 1.53 Impact Factor
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ABSTRACT: A 37.5-kb chromosomal segment with 41.5% G+C content was cloned using genome walking method from Sphingobacterium sp. TN19, a symbiotic strain isolated from the gut of Batocera horsfieldi (Coleoptera, Cerambycidae) larvae. Twenty-three complete and two partial open reading frames (ORFs) were found in this region,
and shared highest identities of 31.6–80.0% (11 of them <60%) to known sequences from the sources shared the common feature—fluid
with low dissolved oxygen levels. These ORFs were organized uniquely in chromosome compared to that from other bacteria, and
putatively involved in xylan and xylose metabolism. To confirm their putative functions, one xylanase gene (xynB19) and one arabinosidase gene (gh43A19), were hetero-expressed in Escherichia coli BL21 (DE3), respectively, and both the recombinant enzymes showed significant enzymatic activities. This result indicates
that xylan degradation is a complex process involving various enzymes, and genome walking is an efficient method to obtain
multiple genes.
Keywords
Batocera horsfieldi
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Sphingobacterium sp.-TN19-Gut-Xylan and xylose metabolism
World Journal of Microbiology and Biotechnology 04/2012; 26(4):761-765. · 1.53 Impact Factor
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ABSTRACT: A xylanase gene, xynA4-2, was obtained from the genome sequence of thermoacidophilic Alicyclobacillus sp. A4 and expressed in Escherichia coli BL21 (DE3). xynA4-2 encodes a mature protein of 411 residues with a calculated molecular weight of 46.8kDa. Based on the amino acid sequence
similarities (highest identity of 61%), the enzyme was confined into glycoside hydrolase family 10. The purified recombinant
XynA4-2 exhibited maximum activity at pH 6.2 and 55°C. The enzyme was stable over a broad pH range, retaining more than 90%
of the original activity at pH 5.8–12.0, 37°C for 1h. The substrate specificity of XynA4-2 was relatively narrow, exhibiting
100, 93, and 35% of the relative activity towards birchwood xylan, oat spelt xylan, and wheat arabinoxylan, respectively.
Supplementation of XynA4-2 to mash caused the reduction of mash filtration rate (5.6%) and viscosity (4.0%). When combined
with the commercial glucanase from Sunson, higher reduction was detected in the filtration rate (12.0%) and viscosity (17.2%).
These favorable properties make XynA4-2 a good candidate in the brewing industry.
Keywords
Alicyclobacillus sp. A4–Xylanase–pH stability–Mash–Viscosity–Filtration rate
World Journal of Microbiology and Biotechnology 04/2012; 27(2):207-213. · 1.53 Impact Factor
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ABSTRACT: A gene, aga-MJ11, encoding an α-galactosidase (EC 3.2.1.22) was cloned from Pedobacter nyackensis MJ11 CGMCC 2503, expressed in Escherichia coli, and biochemically characterized. The gene consisted of 2,163 nucleotides encoding a 720 amino acid–protein with a theoretical
molecular weight of 82.6kDa. The deduced amino acid sequence of Aga-MJ11 shared the highest identity of 51% to an α-galactosidase
from Parabacteroides distasonis (YP_001301506), which belongs to glycoside hydrolase (GH) family 36. Purified recombinant Aga-MJ11-H showed optimal activity
at pH 5.5 and 40°C, was stable at pH 4.0–10.0, retained ~80% of the maximum activity at 30°C (the optimum temperature for
freshwater fish), exhibited tolerance to some proteases, and had a wide substrate specificity (pNPG, melidiose, stachyose
and raffinose). All these features make Aga-MJ11 potentially useful for applications in aquaculture. The enzyme studied in
the present work may represent a novel GH-36 α-galactosidase from the genus Pedobacter.
World Journal of Microbiology and Biotechnology 04/2012; 25(9):1633-1642. · 1.53 Impact Factor
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ABSTRACT: A xylanase gene, xynE2, was cloned from thermoalkaline Anoxybacillus sp. E2 and was expressed in Escherichia coli BL21 (DE3). The gene consisted of 987bp and encoded a 328-residue xylanase with a calculated molecular weight of 38.8kDa.
On the basis of amino acid sequence similarities, this enzyme was assigned as a member of glycoside hydrolase family 10. Purified
recombinant XynE2 showed maximal activity at pH 7.8 and 65°C, and was thermostable at 60°C. The enzyme was highly active and
stable over a broad pH range, showing more than 90% of maximal activity at pH 6.6–pH 8.6 and retaining more than 80% of activity
at pH 4.6–pH 12.0, 37°C for 1h, respectively. These favorable properties make XynE2 a good candidate in the pulp and paper
industries. This is the first report on gene cloning, expression and characterization of a xylanase from the genus Anoxybacillus.
Keywords
Anoxybacillus sp. E2-Xylanase-pH stability-Thermostability
World Journal of Microbiology and Biotechnology 04/2012; 26(5):917-924. · 1.53 Impact Factor
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ABSTRACT: A novel method is proposed to produce both phytase and single-cell protein in recombinant Pichia pastoris fermentation using monosodium glutamate wastewater (MSGW) as the basal medium. Recombinant P. pastoris MR33 transformed with a phytase gene (AppA-m) from Escherichia coli was constructed and showed capability to utilize ammonium as the only nitrogen source. The fermentation medium was optimized
in shake flasks by single-factor test and response surface methodology. A fed-batch system containing 30% MSGW, 50g/l glucose,
1.58g/l CaSO4, 5.18g/l MgSO4 and 6.67g/l KH2PO4 was developed in a 3.7-l bioreactor. The maximum phytase activity in the MSGW medium reached 3,380U/ml, 84.2% of that in
chemically defined medium, and the dry cell weight was 136g/l. The single-cell protein (SCP; 46.66% dry cell weight) contains
a variety of amino acids and is low in fat, which is ideal for utilization in animal feed. Thus, it is feasible to use MSGW
medium for the production of enzymes that can be expressed in P. pastoris.
World Journal of Microbiology and Biotechnology 04/2012; 25(9):1643-1649. · 1.53 Impact Factor
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ABSTRACT: A bacterium with the capability of degrading organphosphorus, identified asPseudomonas pseudoalcaligenes, is isolated from OP-treated soil. The organphosphorus hydrolase OPHC2 from this bacterium has been purified and characterized.
OPHC2 has optimum activity for the reaction at 65 °C and pH 9.0 with methyl parathion as a substrate, it also shows good thermal
and pH stability. Most metal ions and chemicals have no effect on the activity of OPHC2. The analyses of nucleotide sequence
encoding OPHC2 and amino acid sequence of OPHC2 show that there are lower homologies with those of organphosphorus hydrolase
reported in GenBank.
KeywordsPseudomonas pseudoalcaligenes-organphosphorus (OP)-organphosphorus hydrolase (OPH)-purification-properties
Chinese Science Bulletin 04/2012; 49(3):268-272. · 1.32 Impact Factor
