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Inactivation Rate Constant (inactivation + rate_constant)
Selected AbstractsOptimization of fed-batch parameters and harvest time of CHO cell cultures for a glycosylated product with multiple mechanisms of inactivationBIOTECHNOLOGY & BIOENGINEERING, Issue 2 2007Ryan S. Senger Abstract Optimization of fed-batch feeding parameters was explored for a system with multiple mechanisms of product inactivation. In particular, two separate mechanisms of inactivation were identified for the recombinant tissue-type activator (r-tPA) protein. Dynamic inactivation models were written to describe particular r-tPA glycoform inactivation in the presence and absence of free-glucose. A glucose-independent inactivation mechanism was identified, and inactivation rate constants were found dependent upon the presence of glycosylation of r-tPA at N184. Inactivation rate constants of the glucose-dependent mechanism were not affected by glycosylation at N184. Fed-batch optimization was performed for r-tPA production by CHO cell culture in a stirred-tank reactor with glucose, glutamine and asparagine feed. Feeding profiles in which culture supernatant concentrations of free-glucose and amino acids (combined glutamine and asparagine) were used as control variables, were evaluated for a wide variety of set points. Simulation results for a controlled feeding strategy yielded an optimum at set points of 1.51 g L,1 glucose and 1.18 g L,1 of amino acids. Optimization was also performed in absence of metabolite control using fixed feed-flow rates initiate during the exponential growth phase. Fixed feed-flow results displayed a family of optimum solutions along a mass flow rate ratio of 3.15 of glucose to amino acids. Comparison of the two feeding strategies showed a slight advantage of rapid feeding at a fixed flow rate as opposed to metabolite control for a product with multiple mechanisms of inactivation. Biotechnol. Bioeng. 2007;98: 378,390. © 2007 Wiley Periodicals, Inc. [source] CHARACTERISTICS OF MUSCLE FROM TWO SPECIES OF BIGEYE SNAPPER, PRIACANTHUS TAYENUS AND PRIACANTHUS MACRACANTHUSJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2002SOOTTWAT BENJAKUL ABSTRACT Composition and some properties of muscle from two species of bigeye snapper, P. tayenus and P. macracanthus, were investigated. Both species had a similar composition with the same myofibrillar protein content. However, muscle proteins from P. tayenus had higher thermal stability than those from P. macracanthus, as indicated by the higher enthalpy for transitions as well as the lower inactivation rate constant (KD). Upon 15 days of iced storage, natural actomyosin Ca2* -ATP ase and Mg2+ -Ca2+ -ATPase activities decreased, whereas Mg2+ -EGTA-ATPase activity increased, suggesting the denaturation of myosin, actomyosin and troponin/tropomyosin complexes, respectively. Increased surface hydrophobicity and decreased sulfhydryl groups indicated the denaturation possibly occurred via hydrophobic interaction and disulfide formation. Heading and eviscerating offish retarded the denaturation and physicochemical changes of proteins during iced storage. The results indicated that a rapid and proper post harvest handling was of importance to maintain the muscle quality of bigeye snapper. [source] EFFECT OF HIGH HYDROSTATIC PRESSURE ON SPORES OF GEOBACILLUS STEAROTHERMOPHILUS SUSPENDED IN SOYMILKJOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 5 2007YOKIUSHIRDHILGILMARA ESTRADA-GIRÓN ABSTRACT The inactivation of Geobacillus stearothermophilus spores (ATCC 7953) inoculated in soymilk was investigated using high hydrostatic pressure (550, 585 and 620 MPa) in combination with temperature (70, 80 and 90C) for selected times (2 s to 15 min). Inactivation of spores occurred at all selected treatments. Less than 10 CFU/mL of G. stearothermophilus were observed after 7 min of treatment at 620 MPa and 90C. An increase in the inactivation rate constant, at the highest pressure, was observed, resulting in a decrease in D values at all temperatures. D values were calculated as 10.6, 6.2 and 3.5 min for 70, 80 and 90C, respectively after pressurization at 620 MPa. zp values decreased as temperature increased with values ranging from 142 to 238 MPa. The activation energy required for inactivation of G. stearothermophilus spores in soymilk, at the selected treatments, was in the range of 37.9,57.4 kJ/mol. [source] Investigating the potential of Bacillus subtilis ,-amylase as a pressure-temperature-time indicator for high hydrostatic pressure pasteurization processesBIOTECHNOLOGY PROGRESS, Issue 4 2009Tara Grauwet Abstract The potential of Bacillus subtilis ,-amylase (BSA) as a pressure-temperature-time indicator (pTTI) for high pressure pasteurization processing (400,600 MPa; Ti 10,40°C; 1,15 min) was investigated. A stepwise approach was followed for the development of an enzyme-based, extrinsic, isolated pTTI. First, based on literature data on the pressure stability, BSA was selected as a candidate indicator. Next to the accuracy and ease of the measurement of the indicator's response (residual activity) to the pressure treatment, the storage and handling stability of BSA at atmospheric pressure was verified. Second, the stability of BSA at a constant temperature (T) and time in function of pressure (p) was investigated. Solvent engineering was used to shift the inactivation window of BSA in the processing range of interest. Third, the enzyme (1 g/L BSA,MES 0.05 M pH 5.0) was kinetically calibrated under isobaric-isothermal conditions. Time dependent changes in activity could be modeled best by a first-order model. Except for low pressures and high temperatures, a synergistic effect between pressure and temperature could be observed. Based on the model selected to describe the combined p,T-dependency of the inactivation rate constant, an elliptically shaped isorate contour plot could be constructed, illustrating the processing range where BSA can be used to demonstrate temperature gradients. Fourth, the validity of the kinetic model was tested successfully under dynamic conditions similar to those used in food industry. Finally, the indicator was found suitable to demonstrate nonuniformity in two-sectional planes of a vertical, single vessel system. © 2009 American Institute of Chemical Engineers. Biotechnol. Prog., 2009 [source] Optimization of fed-batch parameters and harvest time of CHO cell cultures for a glycosylated product with multiple mechanisms of inactivationBIOTECHNOLOGY & BIOENGINEERING, Issue 2 2007Ryan S. Senger Abstract Optimization of fed-batch feeding parameters was explored for a system with multiple mechanisms of product inactivation. In particular, two separate mechanisms of inactivation were identified for the recombinant tissue-type activator (r-tPA) protein. Dynamic inactivation models were written to describe particular r-tPA glycoform inactivation in the presence and absence of free-glucose. A glucose-independent inactivation mechanism was identified, and inactivation rate constants were found dependent upon the presence of glycosylation of r-tPA at N184. Inactivation rate constants of the glucose-dependent mechanism were not affected by glycosylation at N184. Fed-batch optimization was performed for r-tPA production by CHO cell culture in a stirred-tank reactor with glucose, glutamine and asparagine feed. Feeding profiles in which culture supernatant concentrations of free-glucose and amino acids (combined glutamine and asparagine) were used as control variables, were evaluated for a wide variety of set points. Simulation results for a controlled feeding strategy yielded an optimum at set points of 1.51 g L,1 glucose and 1.18 g L,1 of amino acids. Optimization was also performed in absence of metabolite control using fixed feed-flow rates initiate during the exponential growth phase. Fixed feed-flow results displayed a family of optimum solutions along a mass flow rate ratio of 3.15 of glucose to amino acids. Comparison of the two feeding strategies showed a slight advantage of rapid feeding at a fixed flow rate as opposed to metabolite control for a product with multiple mechanisms of inactivation. Biotechnol. Bioeng. 2007;98: 378,390. © 2007 Wiley Periodicals, Inc. [source] | |||||||||||||