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  • 1
    Electronic Resource
    Electronic Resource
    Mixed-dye staining method for protein detection in polyacrylamide gel electrophoresis using calconcarboxylic acid and rhodamine B (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2412-2415 
    Details
    ISSN: 0173-0835
    Keywords: Protein staining ; Sodium dodecyl sulfate-polyacrylamide gel electrophoresis ; Calconcarboxylic acid ; Rhodamine B ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: We have developed a new mixed-dye protein staining method that is simple, rapid, and sensitive. A freshly prepared mixture of calconcarboxylic acid (NN, 0.02%) and rhodamine B (RB, 0.04%) in 40% methanol / 7% acetic acid, was used as a staining solution. RB acts as an auxiliary agent to inhibit the binding of NN to the gel matrix, reducing the background staining and therefore enhancing the protein staining by NN. This mixed-dye staining method reduces the total staining and destaining time to less than an hour, and increases the sensitivity to 25 ng of bovine serum albumin, which is greater than the 100 ng sensitivity limit of Coomassie Brilliant Blue R-250 (CBBR) staining.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191409
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  • 2
    Electronic Resource
    Electronic Resource
    Application of capillary electrophoresis to amino acid sequencing of peptide (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 510-515 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Micellar electrokinetic chromatography ; Peptide sequencing ; Phenylthiohydantoin-amino acids ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Separations of twenty phenylthiohydantoin (PTH) amino acids, and amino acid derivatives, resulting from the Edman degradation of peptides and proteins, were optimized for peptide sequencing by capillary electrophoresis. Manual sequencing of angiotensin II was performed by Edman degradation and capillary electrophoresis of the PTH amino acid obtained after each cycle. The results were compared with those of an automated conventional protein sequencer. Interfacing capillary electrophoresis with Edman degradation provides an additional option for protein sequencing.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150160184
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  • 3
    Electronic Resource
    Electronic Resource
    Biodegradation of nitrobenzene through a hybrid pathway in Pseudomonas putida (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 625-630 
    Details
    ISSN: 0006-3592
    Keywords: biodegradation ; nitrobenzene ; hybrid strain ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The biodegradation of nitrobenzene was attempted by using Pseudomonas putida TB 103 which possesses the hybrid pathway combining the tod and the tol pathways. Analysis of the metabolic flux of nitrobenzene through the hybrid pathway indicated that nitrobenzene was initially oxidized to cis-1,2-dihydroxy-3-nitrocyclohexa-3,5-diene by toluene dioxygenase in the tod pathway and then channeled into the tol pathway, leading to the complete biodegradation of nitrobenzene. A crucial metabolic step redirecting the metabolic flux of nitrobenzene from the tod to the tol pathway was determined from the genetic and biochemical studies on the enzymes involved in the tol pathway. From these results, it was found that toluate-cis-glycol dehydrogenase could convert cis-1,2-dihydroxy-3-nitrocyclohexa-3,5-diene to catechol in the presence of NAD+ with liberation of nitrite and the reduced form of NAD+ (NADH) into the medium. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260480610
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of salt hydrate pair on lipase-catalyzed regioselective monoacylation of sucrose (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 57 (1998), S. 121-125 
    Details
    ISSN: 0006-3592
    Keywords: sucrose monoester synthesis ; lipase-catalyzed acylation ; water activity (a w) ; regioselectivity ; salt hydrate pair ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Sucrose monoesters of a fatty acid were synthesized by using lipase in a solvent-free system. When lipase from Mucor miehei was used as a catalyst with capric acid as the donor and sugar as the acceptor, sucrose 6-monocaprate was predominantly produced in a yield of 25.3%. The yield of product was significantly increased by the direct addition of a suitable pair of solid salt hydrates to the reaction mixture to control the water activity (aw). Among the salt hydrate pairs investigated, the barium hydroxide, 8/1H2O pair resulted in the highest yield of the product. This salt addition method was also successfully employed for acylation of primary hydroxyl groups in various unprotected mono- and disaccharides such as glucose, galactose, fructose, trehalose, mannose, maltose, and lactose. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 121-125, 1998.
    Additional Material: 3 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    Enhancement effect of water activity on enzymatic synthesis of cephalexin (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 800-806 
    Details
    ISSN: 0006-3592
    Keywords: water activity ; enzyme kinetics ; cephalexin synthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of water activity (aw) of the reaction medium on the enzymatic synthesis of cephalexin (CEX) from 7-amino-3-deacetoxycephalosporanic acid (7-ADCA) and D-α-phenylglycine methyl ester (PGM) was investigated using the α-amino acid ester hydrolase enzyme from Xanthomonas citri. It was found that the synthetic activity of the enzyme and the conversion yield were markedly improved when the aw of the reaction medium was lowered to about 0.97. The water activity depressing agents evaluated were glycerol, sucrose, and sorbitol, and the conversion yields were improved up to 170% with 15% glycerol, 230% with 30% sucrose, and 270% with 20% sorbitol, respectively. The extent of favorable effect of aw on the conversion yield was not the same among the aw depressors, probably due to other unknown interactions between the enzyme and depressors. However, optimal aw values corresponding to the maximum conversion yield coincided for all aw depressors used. The conversion yield of CEX showed an increasing trend with increasing aw up to the optimal aw value (0.96-0.97) which corresponds to the maximum conversion yield and a decreasing trend beyond the optimal aw. There appears to be a delicate balance between the hydrolytic reaction of PGM and synthetic reaction of CEX. The increasing aw-[E · PGM] complex and the branched reaction pathway fluxes from [E · PGM] to PG (D-α-phenyl glycine) and CEX are balanced in such a way that the maximum CEX conversion yield is obtained at aw value of 0.96-0.97. The aw depressors stabilized the enzyme somewhat, but this positive effect was considered to be only a minor contribution to the substantial yield enhancement. The aw depressor effect on viscosity and in turn the mass transfer rate limitation was ruled out since the change in conversion due to the viscosity change was found to be insignificant. © 1993 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420703
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  • 6
    Electronic Resource
    Electronic Resource
    Enzyme-mediated proteolysis of fibrous biopolymers: Dissolution front movement in fibrin or collagen under conditions of diffusive or convective transport (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 89-107 
    Details
    ISSN: 0006-3592
    Keywords: fibrin ; collagen ; proteolysis ; plasminogen ; diffusion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A numerical model based on the convective-diffusive transport of reacting and adsorbing proteolytic enzymes within erodible fibrous biopolymers was used to predict lysis fronts moving across biogels such as fibrin or collagen. The fiber structure and the transport properties of solutes in fibrin (or collagen) were related to the local extent of dissolution within the dissolving structure. An accounting for solubilization of adsorbed species into solution from the eroding fiber phase provided for complete conservation of mass in reacting systems containing over 10 species. At conditions of fibrinolysis typical of clinical situations, the model accurately predicted the dynamic rate of lysis front movement for plasmin, urokinase, and tissue plasminogen activator (tPA)-mediated lysis of fibrin gels measured in vitro. However, under conditions of extremely fast fibrinolysis using high enzyme concentrations, fibrinolytic fronts moved very rapidly (〉0.1 mm/mm) - faster than predicted for diffusionlimited reactions - at nearly constant velocity for over 2 h, indicating non-Fickian behavior. This was due to proteolysis-mediated retraction of dissolving fibrin fibers that resulted in fiber convection and front-sharpening within 3 μm of the reaction front, as observed by digitally enhanced microscopy. In comparing the model to fibrinolysis measurements using human lys77-plasmin, the average first order rate constant for non-crosslinked fibrin bond cleavage by fibrin-bound plasmin was calculated to be 5s-1 assuming that 10 cleavages per fibrin monomer were required to solubilize each monomer. The model accurately predicted lysis front movement using pressure-driven permeation of plasmin or urokinase into fibrin as well as literature data obtained under well- mixed conditions for tPA-mediated fibrinolysis. This numerical formulation provides predictive capability for optimization of proteolytic systems which include thrombolytic therapy, wound healing, controlled drug release, and tissue engineering applications. © 1995 John Wiley & Sons, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260480203
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  • 7
    Electronic Resource
    Electronic Resource
    Extractive separation of penicillin G by facilitated transport via carrier supported liquid membranes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 527-534 
    Details
    ISSN: 0006-3592
    Keywords: penicillin G ; liquid membrane ; facilitated transport ; separation process ; Amberlite LA-2 ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The facilitated transport of penicillin G (Pen G), through a supported liquid membrane with Amberlite LA-2 dissolved in 1-decanol, supported on a microporous polypropylene membrane, were studied. The distribution coefficient was obtained from a batch extraction experiment. The effects of flow rate, carrier concentration, initial concentration of Pen G, and the pH of feed and stripping phases on the transport rate of Pen G through the supported liquid membrane were also investigated. The results are in agreement with theoretical predictions, and it is demonstrated that the transport of Pen G through the supported liquid membrane is controlled simultaneously by mass transfer across both aqueous and liquid membranes. © 1993 John Wiley & Sons, Inc.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420417
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  • 8
    Electronic Resource
    Electronic Resource
    Amplification of toluene dioxygenase genes in a hybrid Pseudomonas strain to enhance the biodegradation of benzene, toluene, and p-xylene mixture (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 488-494 
    Details
    ISSN: 0006-3592
    Keywords: biodegradation ; gene amplification ; hybrid strain ; benzene ; toluene ; xylene ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A hybrid metabolic pathway through which benzene, toluene, and p-xylene (BTX) mixture could be simultaneously mineralized was previously constructed in Pseudomonas putida TB101 (Lee, Roh, Kim, Biotechnol. Bioeng 43: 1146-1152, 1994). In this work, we improved the performance of the hybrid pathway by cloning the todC1C2BA genes in the broad-host-range multicopy vector RSF1010 and by introducing the resulting plasmid pTOL037 into P. putida mt-2 which harbors the archetypal TOL plasmid. As a result, a new hybrid strain, P. putida TB103, possessing the enhanced activity of toluene dioxygenase in the hybrid pathway was constructed. The degradation rates of benzene, toluene, and p-xylene by P. putida TB103 were increased by about 9.3-, 3.7-, and 1.4-fold, respectively, compared with those by previously constructed P. putida TB101. Apparently, this improved capability of P. putida TB103 for the degradation of BTX mixture resulted from the amplification of the todC1C2BA genes. Furthermore, a relatively long lag period for benzene degradation observed when P. putida TB101 was used for the degradation of BTX mixture at low dissolved oxygen (DO) tension disappeared when P. putida TB103 was employed. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260450605
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  • 9
    Electronic Resource
    Electronic Resource
    Production of a high viscosity polysaccharide, methylan, in a novel bioreactor (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 54 (1997), S. 115-121 
    Details
    ISSN: 0006-3592
    Keywords: Methylobacterium organophilum ; high viscosity polysaccharide ; methylan ; multidisk mixer ; bioreactor ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of shear stress on the production of a high viscosity polysaccharide, methylan, from methanol by Methylobacterium organophilum was investigated by using a multidisk mixer. It was observed in the multidisk mixer with defined shear stresses that the specific production rate of methylan increased gradually with increasing shear stress up to 30 Pa, and the production rate was constant beyond 30 Pa. This result suggested that the limited mass transfer from the medium into cells reduced methylan production. A novel bioreactor that provided the large volume of a high shear region was used to increase methylan production. Fed-batch cultures in the novel bioreactor were performed by the dissolved oxygen-stat method of methanol. When 1.13 g/L ammonium ion was added, the concentrations of cells of methylan were 31 and 20.6 g/L, respectively. The productions of cells and methylan in our designed bioreactor were 20 and 50% higher than those obtained in a conventional fermentor. The methylan content reached a maximum of 20.7 g/L in the bioreactor and the viscosity of the fermentation broth was 127 Pa · s, which corresponds to 68 g/L as a xanthan. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 115-121, 1997.
    Additional Material: 7 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Experimental optimization of fed-batch culture for poly-β-hydroxybutyric acid production (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 56 (1997), S. 697-705 
    Details
    ISSN: 0006-3592
    Keywords: poly-β-hydroxybutyric acid ; Alcaligenes eutrophus ; fed-batch culture ; high cell density culture ; optimization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The optimal feed rate profiles of glucose and ammonium hydroxide were calculated using a proposed model, and implemented for the production of poly-β-hydroxybutyric acid (PHB) by Alcaligenes eutrophus. By implementing these optimal feed rates with a high glucose feed concentration of 700 g/L and an ammonium hydroxide concentration of 7%(w/w), it was possible to achieve a high final cell concentration of 141 g/L and a high PHB concentration of 105 g/L in 40 h of fed-batch operation. The PHB productivity was as high as 2.63 g/(L hr). © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 697-705, 1997.
    Additional Material: 7 Ill.
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