Check out our New Publishers' Select for Free Articles

Applied Biochemistry and Biotechnology: Part A: Enzyme Engineering and Biotechnology (v.163, #1)

Behavior of Wild-type and Transfected S2 Cells Cultured in Two Different Media by Fabiana R. X. Batista; Kátia N. Greco; Renato M. Astray; Soraia A. C. Jorge; Elisabeth F. P. Augusto; Carlos A. Pereira; Ronaldo Z. Mendonça; Ângela M. Moraes (pp. 1-13).

An animal protein-free medium composed of IPL-41 containing 6 g L⁻¹ yeastolate ultrafiltrate, 10 g L⁻¹ glucose, 2 g L⁻¹ lactose, 5 g L⁻¹ glutamine, 1% lipid emulsion, and 0.1% Pluronic F-68 was used for producing recombinant proteins in batch mode employing two cell lines, S2AcRVGP2k expressing the G glycoprotein from rabies virus (RVGP) and S2AcHBsAgHy-9C expressing the surface antigen of hepatitis B virus (HBsAg), both obtained from Drosophila melanogaster S2 cells. Growth of wild-type S2 cells was also evaluated in the same medium. Cell behavior in the tested medium was compared to that verified in Sf900 II®. The results show that in shake flasks, S2AcRVGP2k and S2AcHBsAgHy-9C cells reached around 2 × 10⁷ cells mL⁻¹ in both media. In supplemented IPL-41 and Sf900 II® media, S2AcRVGP2k cells produced 367 ng RVGP mL⁻¹ and 638 ng RVGP mL⁻¹, respectively, while S2AcHBsAgHy-9C cells correspondently produced 573 ng HBsAg mL⁻¹ and 322 ng HBsAg mL⁻¹ in the mentioned media. In stirred tanks, S2AcRVGP2k cells reached 3 × 10⁷ cells mL⁻¹ and produced up to 758 ng RVGP mL⁻¹. In general, glucose was consumed by cells, while lactate and ammonia were produced.

Keywords: S2 cells; Metabolism; RVGP; HBsAg; Animal protein-free medium

Influence of Different Substrates on the Production of a Mutant Thermostable Glucoamylase in Submerged Fermentation by Fabiana Carina Pavezzi; Andréia A. Jacomassi Carneiro; Daniela Alonso Bocchini-Martins; Heloiza Ferreira Alves-Prado; Henrique Ferreira; Paula M. Martins; Eleni Gomes; Roberto da Silva (pp. 14-24).

Three mutations, Ser54→Pro, Thr314→Ala, and His415→Tyr, were identified in Aspergillus awamori glucoamylase gene expressed by Saccharomyces cerevisiae. The mutant glucoamylase (GA) was substantially more thermostable than a wild-type GA at 70 °C, with a 3.0 KJ mol⁻¹ increase in the free energy of thermo-inactivation. The effect of starch from different botanical sources on the production of this GA was measured in liquid fermentation using commercial soluble starch, cassava, potato, and corn as the carbon source. The best substrate for GA production was the potato starch showing an enzymatic activity of 6.6 U/mL. The commercial soluble starch was also a good substrate for the enzyme production with 6.3 U/mL, followed by cassava starch and corn starch with 5.9 and 3.0 U/mL, respectively. These results showed a significant difference on GA production related to the carbon source employed. The mutant GA was purified by acarbose–Sepharose affinity chromatography; the estimated molecular mass was 100 kDa. The mutant GA exhibited optimum activity at pH 4.5 and an optimum temperature of 65 °C.

Keywords: Mutant glucoamylase; Thermostable enzyme; Production; Purification; Corn starch; Potato starch; Cassava starch; Thermo-inactivation

Production and Characterization of Cellobiohydrolase from a Novel Strain of Penicillium purpurogenum KJS506 by Kyoung-Mi Lee; Ah-Reum Joo; Marimuthu Jeya; Kyoung-Min Lee; Hee-Jung Moon; Jung-Kul Lee (pp. 25-39).

A high cellobiohydrolase (CBH)-producing strain was isolated and identified as Penicillium purpurogenum KJS506 according to the morphology and comparison of internal transcribed spacer rDNA gene sequence. When rice straw and corn steep powder were used as carbon and nitrogen sources, respectively, a maximum CBH activity of 2.6 U mg-protein⁻¹, one of the highest among CBH-producing microorganisms, was obtained. The optimum temperature and pH for CBH production were 30 °C and 4.0, respectively. The increased production of CBH in P. purpurogenum culture at 30 °C was confirmed by two-dimensional electrophoresis followed by MS/MS sequencing of the partial peptide. The internal amino acid sequences of P. purpurogenum CBH showed a significant homology with hydrolases from glycoside hydrolase family 7. The extracellular CBH was purified to homogeneity by sequential chromatography of P. purpurogenum culture supernatants on a DEAE-sepharose column, a gel filtration column, and then on a Mono Q column with fast-protein liquid chromatography. The purified CBH was a monomeric protein with a molecular weight of 60 kDa and showed broad substrate specificity with maximum activity towards p-nitrophenyl β-d-cellobiopyranoside. P. purpurogenum CBH showed t _1/2 value of 4 h at 60 °C and V _max value of 11.9 μmol min⁻¹ mg-protein⁻¹ for p-nitrophenyl-d-cellobiopyranoside. Although CBHs have been reported, the high specific activity distinguishes P. purpurogenum CBH.

Keywords: Cellobiohydrolase; Enzyme production; Glycoside hydrolase; Penicillium purpurogenum ; Purification

Enzyme Production by Solid Substrate Fermentation of Pleurotus ostreatus and Trametes versicolor on Tomato Pomace by Donata Iandolo; Alessandra Piscitelli; Giovanni Sannia; Vincenza Faraco (pp. 40-51).

A process of solid state fermentation (SSF) on tomato pomace was developed with the white-rot fungi Pleurotus ostreatus and Trametes versicolor, using sorghum stalks as support. Operative parameters (humidity, water activity, and size of substrate particles) guaranteeing a good colonization of tomato pomace by both fungi were defined and conditions for production at high titers of the industrially relevant enzymes laccase, xylanase and protease were identified. Significant laccase activity levels (up to 36 U g⁻¹ dry matter) were achieved without any optimization of culture conditions, neither by nutrient addition nor by O₂ enrichment. Furthermore, protease activity levels up to 34,000 U g⁻¹ dry matter were achieved, being higher than those reported for the fungi typically considered as the best protease producers such as Aspergillus strains. Moreover, as one of the most significant results of this study, analysis of P. ostreatus tomato SSF samples by zymogram revealed two bands with laccase activity which had not been detected so far.

Keywords: Fungi; Solid state fermentation; Laccase; Xylanase; Protease

Cloning and Characterization of a Sucrose Isomerase from Erwinia rhapontici NX-5 for Isomaltulose Hyperproduction by Sha Li; Heng Cai; Yujia Qing; Ben Ren; Hong Xu; Hongyang Zhu; Jun Yao (pp. 52-63).

The sucrose isomerase (SIase) gene from an efficient strain of Erwinia rhapontici NX-5 for isomaltulose hyperproduction was cloned and overexpressed in Escherichia coli. Protein sequence alignment revealed that SIase was a member of the glycoside hydrolase 13 family. The molecular mass of the purified recombinant protein was estimated at 66 kDa by SDS-PAGE. The SIase had an optimal pH and temperature of 5.0 and 30 °C, respectively, with a K _m of 257 mmol/l and V _max of 48.09 μmol/l/s for sucrose. To the best of our knowledge, the recombinant SIase has the most acidic optimum pH for isomaltulose synthesis. When the recombinant E. coli (pET22b- palI) cells were used for isomaltulose synthesis, almost complete conversion of sucrose (550 g/l solution) to isomaltulose was achieved in 1.5 h with high isomaltulose yields (87%). The immobilized E. coli cells remained stable for more than 30 days in a “batch”-type enzyme reactor. This indicated that the recombinant SIase could continuously and efficiently produce isomaltulose.

Keywords: Erwinia rhapontici ; Isomaltulose; Sucrose isomerase; Sucrose; Trehalulose

Use of Highly Purified and Mixed Antibodies for Simultaneous Detection of Multiple Protein Species Released from Mitochondria upon Induction of the Permeability Transition by Takenori Yamamoto; Mizuki Ohashi; Sho Mizutani; Yuuya Yoshimura; Eriko Obana; Hiroshi Terada; Yasuo Shinohara (pp. 64-70).

Concomitant with the induction of the mitochondrial permeability transition (PT), cytochrome c is released from mitochondria into the cytosol where it triggers subsequent steps of cellular apoptosis. Thus, inducers of the mitochondrial PT would become “seed compounds” of regulators of apoptosis. However, when we examine the actions of certain chemicals on the release of mitochondrial cytochrome c, the behaviors of not only cytochrome c but also multiple mitochondrial protein species must be carefully examined because the mitochondrial PT and release of proteins from mitochondria occur in diverse manners. In the present study, we examined whether it is possible to measure the behaviors of multiple protein species in a single experiment using purified and mixed antibodies. The results obtained clearly indicate that this procedure would be applicable for high-throughput screening of regulators of apoptosis. Further requirements necessary for the establishment of a useful screening system for apoptosis regulators are discussed.

Keywords: Mitochondria; Permeability transition; Protein release; Cytochrome c; Western blotting

Efficient Enzymatic Production of the Bacterial Second Messenger c-di-GMP by the Diguanylate Cyclase YdeH from E. coli by Franziska Zähringer; Claudia Massa; Tilman Schirmer (pp. 71-79).

Cyclic di-GMP (c-di-GMP) is an almost universal bacterial second messenger involved in the regulation of cell surface-associated traits and the persistence of infections. GGDEF and EAL domain-containing proteins catalyse c-di-GMP synthesis and degradation, respectively. We report the enzymatic large-scale synthesis of c-di-GMP, making use of the GGDEF domain-containing protein YdeH from Escherichia coli. Overexpression and purification of YdeH have been established, and the conditions for c-di-GMP synthesis were optimised. In contrast to the chemical synthesis of c-di-GMP, enzymatic c-di-GMP production is a one-step reaction that can easily be performed with the equipment of a standard biochemical lab. The protocol allows the production of milligram amounts of c-di-GMP within 1 day and paves the way for extensive biochemical and biophysical studies on c-di-GMP-mediated processes.

Keywords: c-di-GMP; Diguanylate cyclase; GGDEF domain; Enzymatic synthesis; E. coli

Expression and Secretion of a CB4-1 scFv–GFP Fusion Protein by Fission Yeast by Julia Maria Naumann; Gabriele Küttner; Matthias Bureik (pp. 80-89).

There is a rapidly growing demand for fluorescent single-chain Fv (scFv) antibody fragments for many applications. Yeasts have developed into attractive hosts for recombinant production of these functionalized proteins because they provide several advantages over prokaryotes and higher eukaryotes as expression systems, e.g., being capable of high-level secretion of heterologous proteins. In this study, we report Schizosaccharomyces pombe as a new host organism for secretory production of scFv-green fluorescent protein (GFP) fusions and compare it with previously described yeast expression systems. We cloned a plasmid for the expression and secretion of the anti-p24 (human immunodeficiency virus 1) CB4-1 scFv fused to GFP. After expression of the scFv–GFP fused to an N-terminal Cpy1 secretion signal sequence, fluorescence microscopy of living yeast cells indicated that the heterologous protein entered the secretory pathway. Western blot analysis of cell-free culture supernatants confirmed that the scFv–GFP was efficiently secreted with yields up to 5 mg/L. In addition, fluorescence measurements of culture supernatants demonstrated that the GFP moiety of the scFv–GFP protein is fully functional after secretion. Our data suggest that S. pombe has the potential for being used as alternative expression host in recombinant antibody fragment production by ensuring efficient protein processing and secretion.

Keywords: Fission yeast (Schizosaccharomyces pombe); Heterologous protein production; Secretion; Cpy1; Recombinant antibodies; Single-chain Fv (scFv) fragments; CB4-1; Green fluorescent protein (GFP); Functionalized scFv

Evaluation of Target Efficiencies for Solid–Liquid Separation Steps in Biofuels Production by Vadim Kochergin; Keith Miller (pp. 90-101).

Development of liquid biofuels has entered a new phase of large scale pilot demonstration. A number of plants that are in operation or under construction face the task of addressing the engineering challenges of creating a viable plant design, scaling up and optimizing various unit operations. It is well-known that separation technologies account for 50–70% of both capital and operating cost. Additionally, reduction of environmental impact creates technological challenges that increase project cost without adding to the bottom line. Different technologies vary in terms of selection of unit operations; however, solid–liquid separations are likely to be a major contributor to the overall project cost. Despite the differences in pretreatment approaches, similar challenges arise for solid–liquid separation unit operations. A typical process for ethanol production from biomass includes several solid–liquid separation steps, depending on which particular stream is targeted for downstream processing. The nature of biomass-derived materials makes it either difficult or uneconomical to accomplish complete separation in a single step. Therefore, setting realistic efficiency targets for solid–liquid separations is an important task that influences overall process recovery and economics. Experimental data will be presented showing typical characteristics for pretreated cane bagasse at various stages of processing into cellulosic ethanol. Results of generic material balance calculations will be presented to illustrate the influence of separation target efficiencies on overall process recoveries and characteristics of waste streams.

Keywords: Solid–liquid separations; Ethanol production; Lignocellulosic biomass

Esterification Synthesis of Ethyl Oleate in Solvent-Free System Catalyzed by Lipase Membrane from Fermentation Broth by Wei-Na Li; Bi-Qiang Chen; Tian-Wei Tan (pp. 102-111).

In this study, the immobilized lipase was prepared by fabric membrane adsorption in fermentation broth. The lipase immobilization method in fermentation broth was optimized on broth activity units and pH adjustments. The viscose fermentation broth can be used with a certain percentage of dilution based on the original broth activity units. The fermentation broth can be processed directly without pH adjustment. In addition, the oleic acid ethyl ester production in solvent-free system catalyzed by the immobilized lipase was optimized. The molar ratio of ethanol to oil acid, the enzyme amount, the molecular amount, and the temperature were 1:1, 12% (w/w), 9% (w/w)(based the total amount of reaction mixture), and 30 °C, respectively. Finally, the optimal condition afforded at least 19 reuse numbers with esterification rate above 80% under stepwise addition of ethanol. Due to simple lipase immobilization preparation, acceptable esterification result during long-time batch reactions and lower cost; the whole process was suitable for industrial ethyl oleate production.

Keywords: Candida sp. 99–125; Immobilized lipase membrane; Fermentation broth; Esterification; Oleic acid; Solvent-free system

Identification of a Keratinase-Producing Bacterial Strain and Enzymatic Study for Its Improvement on Shrink Resistance and Tensile Strength of Wool- and Polyester-Blended Fabric by Shao-Bo Cai; Zheng-Hua Huang; Xing-Qun Zhang; Zhang-Jun Cao; Mei-Hua Zhou; Feng Hong (pp. 112-126).

A wool-degrading bacterium was isolated from decomposition wool fabrics in China. The strain, named 3096-4, showed excellent capability of removing cuticle layer of wool fibers, as demonstrated by removing cuticle layer completely within 48 h. According to the phenotypic characteristics and 16S rRNA profile, the isolate was classified as Pseudomonas. Bacteria growth and keratinase activity of the isolate were determined during cultivation on raw wool at different temperatures, initial pH, and rotation speed using orthogonal matrix method. Maximum growth and keratinase activity of the bacterium were observed under the condition including 30 °C, initial pH 7.6, and rotational speeds 160 rpm. The keratinase-containing crude enzyme prepared from 3096-4 was evaluated in the treatment of wool fabrics. The optimal condition of our enzymatic improvement of shrink resistance was the combination of 30 °C, initial pH 7.6, and rotation speeds 160 rpm. After the optimized treatment, the wool fabrics felting shrink was 4.1% at 6 h, and textile strength was not lost.

Keywords: Pseudomonas ; Keratinase; Wool fabrics; Shrink resistance

AnSBBR Applied to a Personal Care Industry Wastewater Treatment: Effects of Fill Time, Volume Treated Per Cycle, and Organic Load by José Alberto Domingues Rodrigues; Ricardo Polisaitis Oliveira; Suzana Maria Ratusznei; Marcelo Zaiat; Eugenio Foresti (pp. 127-142).

A study was performed regarding the effect of the relation between fill time, volume treated per cycle, and influent concentration at different applied organic loadings on the stability and efficiency of an anaerobic sequencing batch reactor containing immobilized biomass on polyurethane foam with recirculation of the liquid phase (AnSBBR) applied to the treatment of wastewater from a personal care industry. Total cycle length of the reactor was 8 h (480 min). Fill times were 10 min in the batch operation, 4 h in the fed-batch operation, and a 10-min batch followed by a 4-h fed batch in the mixed operation. Settling time was not necessary since the biomass was immobilized and decant time was 10 min. Volume of liquid medium in the reactor was 2.5 L, whereas volume treated per cycle ranged from 0.88 to 2.5 L in accordance with fill time. Influent concentration varied from 300 to 1,425 mg COD/L, resulting in an applied volumetric organic load of 0.9 and 1.5 g COD/L.d. Recirculation flow rate was 20 L/h, and the reactor was maintained at 30 °C. Values of organic matter removal efficiency of filtered effluent samples were below 71% in the batch operations and above 74% in the operations of fed batch followed by batch. Feeding wastewater during part of the operational cycle was beneficial to the system, as it resulted in indirect control over the conversion of substrate into intermediates that would negatively interfere with the biochemical reactions regarding the degradation of organic matter. As a result, the average substrate consumption increased, leading to higher organic removal efficiencies in the fed-batch operations.

Keywords: AnSBBR; Personal care industry wastewater; Fill time; Feed volume; Organic load

Enhanced Enzymatic Saccharification of Barley Straw Pretreated by Ethanosolv Technology by Youngran Kim; Anna Yu; Minhee Han; Gi-wook Choi; Bongwoo Chung (pp. 143-152).

The fermentable sugars in lignocellulosic biomass are derived from cellulose and hemicellulose, which are not readily accessible to enzymatic saccharification because of their recalcitrance. An ethanosolv pretreatment method was applied for the enzymatic saccharification of barley straw with an inorganic acid. The effects of four process variables (temperature, time, catalyst dose, and ethanol concentration) on the barley straw pretreatment were analyzed over a broad range using a small composite design and a response surface methodology. The yield of the residual solid and composition of the solid fraction differed as ethanosolv conditions varied within the experimental range. A glucan recovery, xylan recovery, and delignification were 85%, 14%, and 69% at center point conditions (170°C, 60 min, 1.0% (w/w) H₂SO₄, and 50% (w/w) ethanol), respectively. Ethanosolv pretreatment removed lignin effectively. Additionally, the highest enzymatic digestibility of 85.3% was obtained after 72 h at center point conditions.

Keywords: Organosolv pretreatment; Ethanosolv; Lignocellulose; Barley straw; Bioethanol

Co-immobilization Mechanism of Cellulase and Xylanase on a Reversibly Soluble Polymer by Zidong Xu; Yelian Miao; Jie Yu Chen; Xuejian Jiang; Lijun Lin; Pingkai Ouyang (pp. 153-161).

Cellulase and xylanase from Trichoderma reesei were immobilized simultaneously on Eudragit L-100, a reversibly soluble polymer. The effects of polymer concentration and polymer precipitation pH on enzyme activity recovery were investigated at an enzyme complex concentration of 1%. The immobilization mechanism of cellulase and xylanase on the polymer was discussed. An activity recovery of 75% and 59% was obtained for the cellulase and the xylanase, respectively, under the condition of a polymer concentration at 2% and a polymer precipitation pH at 4.0. Most zymoproteins might be connected to the polymer by electrostatic attraction in a medium of pH 4.8. In addition, the covalent coupling between the zymoproteins and the polymer was demonstrated by the infrared spectrograms. It was suggested that dehydration–condensation reaction occurred between the zymoproteins and the polymer during the immobilization.

Keywords: Immobilization; Cellulase; Xylanase; Covalent coupling; Ionic adsorption

Effects of Low-Shear Modeled Microgravity on the Characterization of Recombinant β-D-Glucuronidase Expressed in Pichia pastoris by Feng Qi; DaZhang Dai; Yanli Liu; Imdad Kaleem; Chun Li (pp. 162-172).

In this study, we used a high-aspect-ratio vessel (HARV), which could model environment of microgravity on ground to investigate for the first time the effects of low-shear modeled microgravity (LSMMG) on the characterization of recombinant β-D-glucuronidase expressed in Pichia pastoris. The β-D-glucuronidase gene (GenBank accession no. EU095019) derived from Penicillium purpurogenum Li-3 encoding β-D-glucuronidase (PGUS) was expressed in P. pastoris GS115 in two different environments of LSMMG and normal gravity (NG). Results manifested that both LSMMG and NG conditions had insignificant effects on temperature and pH activity (optimal temperature and pH were 55 and 5.0 °C, respectively) and characteristic stability of recombinant PGUS. However, the catalytic activity of recombinant PGUS expressed under LSMMG was less affected by metal ions and EDTA as compared with that of NG. Furthermore, K _m value of the recombinant PGUS expressed under LSMMG was nearly one fifth of that under NG (1.72 vs. 7.72), whereas catalytic efficiency (k _cat/K _m) of PGUS expressed under LSMMG (13.55) was 3.7 times higher than that of NG (3.61). The results initially reveal the significant alterations in catalytic properties of recombinant enzyme in response to LSMMG environment and have potential application in bioprocessing and biocatalysis.

Keywords: Low-shear modeled microgravity (LSMMG); Normal gravity (NG); Pichia pastoris ; Recombinant PGUS

Integrated Downstream Processing of Lactoperoxidase from Milk Whey Involving Aqueous Two-Phase Extraction and Ultrasound-Assisted Ultrafiltration by K. E. Nandini; Navin K. Rastogi (pp. 173-185).

The present work involves the adoption of an integrated approach for the purification of lactoperoxidase from milk whey by coupling aqueous two-phase extraction (ATPE) with ultrasound-assisted ultrafiltration. The effect of system parameters of ATPE such as type of phase system, polyethylene glycol (PEG) molecular mass, system pH, tie line length and phase volume ratio was evaluated so as to obtain differential partitioning of contaminant proteins and lactoperoxidase in top and bottom phases, respectively. PEG 6000-potassium phosphate system was found to be suitable for the maximum activity recovery of lactoperoxidase 150.70% leading to 2.31-fold purity. Further, concentration and purification of enzyme was attempted using ultrafiltration. The activity recovery and purification factor achieved after ultrafiltration were 149.85% and 3.53-fold, respectively. To optimise productivity and cost-effectiveness of integrated process, influence of ultrasound for the enhancement of permeate flux during ultrafiltration was also investigated. Intermittent use of ultrasound along with stirring (2 min acoustic and 2 min stirring) resulted in increased permeate flux from 0.94 to 2.18 l/m² h in comparison to the ultrafiltration without ultrasound. The use of ultrasound during ultrafiltration resulted in increase in flux, but there was no significant change in activity recovery and purification factor. The integrated approach involving ATPE and ultrafiltration may prove to be a feasible method for the downstream processing of lactoperoxidase from milk whey.

Keywords: Lactoperoxidase; Ultrasound; Ultrafiltration; ATPE; Purification; Integrated process

Redesign the α/β Fold to Enhance the Stability of Mannanase Man23 from Bacillus subtilis by Hai-Yan Zhou; Hong-Ya Pan; Li-Qun Rao; Yong-Yao Wu (pp. 186-194).

In this work, we engineered the α/β fold of mannanase Man23 based on its molecular structure analysis to obtain more stable variants. By introducing 31 single-site mutations in the α/β fold and shuffling them, the incorporation of four mutations (K178R, K207R, N340R, and S354R) displayed a good balance between high activity and stability at higher temperature and broader pH. This quartet variant was characterized by an almost threefold increased activity and a sevenfold increased stability compared to native mannanase Man23. Our results suggest that such work is safe to increase our target protein stability with no loss of activity.

Keywords: Mannanase; Protein stability; Rational design; α/β Fold

Accumulation of Poly[(R)-3-hydroxyalkanoates] in Enterobacter cloacae SU-1 During Growth with Two Different Carbon Sources in Batch Culture by Antony V. Samrot; Reddy B. Avinesh; Sahaya D. Sukeetha; P. Senthilkumar (pp. 195-203).

Polyhydroxyalkanoates (PHAs) are polymers of hydroxyalkanoate, which are accumulated by many bacteria as food storage material under excess carbon source and limited nitrogen source. In our study, Enterobacter cloacae SU-1 isolated from the rhizospheric soil of Arachis hypogea was allowed to grow as batch culture in minimal media containing either glucose or lactose, and the pattern of PHA accumulation by E. cloacae SU-1 was studied. E. cloacae SU-1 was found to accumulate 94% of PHA/dry weight of the organism in 8 g/l lactose-containing medium. When the monomeric units of PHA of E. cloacae SU-1 was analyzed by gas chromatography, it was also found to accumulate medium chain length PHA 3-hydroxyoctanoate (3HO)/3-hydroxyhexanoate (3HH) in the presence of glucose and lactose, but the ratio of these monomers differed as 11:1 and 6:1, respectively.

Keywords: Polyhydroxyalkanoates (PHA); 3-hydroxyhexanoate (3HH); 3-Hydroxyoctanoate (3HO); Arachis hypogea ; Enterobacter cloacae SU-1; Gas chromatography (GC)

Sections

Personal tools

Applied Biochemistry and Biotechnology: Part A: Enzyme Engineering and Biotechnology (v.163, #1)

Sections

Personal tools

Local resources

Applied Biochemistry and Biotechnology: Part A: Enzyme Engineering and Biotechnology (v.163, #1)