Effects of temperature on the hydrolysis of lactose by immobilized β‐galactosidase in a capillary bed reactor

Peterson, Ronnie; Hill, Charles G.; Amundson, C. H.

doi:10.1002/bit.260340403

Cited by 26 publications

(11 citation statements)

References 6 publications

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“…With time progress, enzyme was deactivated and consequently, the DH was reduced at 45 °C. Similar explanation was given in several cases (44,45). The value of maximum reaction velocity of enzymatic hydrolysis (v max ) was increased almost 2.6-fold by increasing the temperature from 25 to 40 °C.…”

Section: Enzymatic Digestionsupporting

confidence: 79%

Production of Hypoallergenic Antibacterial Peptides from Defatted Soybean Meal by a Membrane Associated Bioreactor: A Bioprocess Engineering Study with Comprehensive Product Characterization

Nath

Szécsi

Csehi

et al. 2017

Food Technol. Biotechnol.

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SummaryHypoallergenic antibacterial low-molecular-mass peptides were produced from defatted soybean meal in a membrane bioreactor. In the fi rst step, soybean meal proteins were digested with trypsin in the bioreactor, operated in batch mode. For the tryptic digestion of soybean meal protein, optimum initial soybean meal concentration of 75 g/L, temperature of 40 °C and pH=9.0 were determined. Aft er enzymatic digestion, low-molecular-mass peptides were purifi ed with cross-fl ow fl at sheet membrane (pore size 100 μm) and then with tubular ceramic ultrafi ltration membrane (molecular mass cut-off 5 kDa). Eff ects of transmembrane pressure and the use of a static turbulence promoter to reduce the concentration polarization near the ultrafi ltration membrane surface were examined and their positive eff ects were proven. For the fi ltration with ultrafi ltration membrane, transmembrane pressure of 3·10 5 Pa with 3-stage discontinuous diafi ltration was found optimal. The molecular mass distribution of purifi ed peptides using ultrafi ltration membrane was determined by a liquid chromatography-electrospray ionization quadrupole time-of-fl ight mass spectrometry setup. More than 96 % of the peptides (calculated as relative frequency) from the ultrafi ltration membrane permeate had the molecular mass M≤1.7 kDa and the highest molecular mass was found to be 3.1 kDa. The decrease of allergenic property due to the tryptic digestion and membrane fi ltration was determined by an enzyme-linked immunosorbent assay and it was found to exceed 99.9 %. It was also found that the peptides purifi ed in the ultrafi ltration membrane promoted the growth of Pediococcus acidilactici HA6111-2 and they possessed antibacterial activity against Bacillus cereus.

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Section: Enzymatic Digestionsupporting

confidence: 79%

Production of Hypoallergenic Antibacterial Peptides from Defatted Soybean Meal by a Membrane Associated Bioreactor: A Bioprocess Engineering Study with Comprehensive Product Characterization

Nath

Szécsi

Csehi

et al. 2017

Food Technol. Biotechnol.

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“…The hydrolysis of lactose by immobilized β -galactosidase has also been studied in a continuous flow capillary bed reactor by various temperatures. Based on the observed thermal deactivation rate constants, at an operating temperature of 40°C, only 10% of the enzyme activity loss could be there in one year [125]. …”

Section: Applications Of Immobilized β-Galactosidasementioning

confidence: 99%

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

2010

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The enzyme β-galactosidase can be obtained from a wide variety of sources such as microorganisms, plants, and animals. The use of β-galactosidase for the hydrolysis of lactose in milk and whey is one of the promising enzymatic applications in food and dairy processing industries. The enzyme can be used in either soluble or immobilized forms but the soluble enzyme can be used only for batch processes and the immobilized form has the advantage of being used in batch wise as well as in continuous operation. Immobilization has been found to be convenient method to make enzyme thermostable and to prevent the loss of enzyme activity. This review has been focused on the different types of techniques used for the immobilization of β-galactosidase and its potential applications in food industry.

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“…Models based on complex mechanisms contain a number of parameters that exceed the possibility of their experimental determination; therefore, models based on simple ®rst-order kinetics or two-stage series mechanisms have been frequently used, despite its obvious simpli®ca-tion [11,12,13]. Reactor design considering enzyme inactivation frequently disregard the effect of substrates and products on inactivation rate constants [5,14,15,16] or is based on global inactivation rate constants determined under particular operating conditions [3,6,17], not allowing to discriminate the individual modulation effects. Only in a few cases, protection by substrate has been evaluated and considered for reactor design [2,18,19,20] and, even in fewer, product modulation has been included [21,22].…”

Section: List Of Symbolsmentioning

confidence: 99%

“…In practice, very narrow ranges of temperature can be used [4], which makes operation cumbersome; besides, proper reactor design requires of temperature explicit functions for kinetic [6] and inactivation [7] parameters. The ®rst strategy is based on compensating enzyme decay by decreasing¯ow rate, since to keep substrate conversion (product quality) constant, the ratio of enzyme activity tō ow rate must remain constant.…”

Section: List Of Symbolsmentioning

confidence: 99%

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Design of immobilized enzyme reactors for the continuous production of fructose syrup from whey permeate

Illanes

Wilson

Raiman

1999

Bioprocess Engineering

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Biocatalyst inactivation is inherent to continuous operation of immobilized enzyme reactors, meaning that a strategy must exist to ensure a production of uniform quality and constant throughput. Flow rate can be pro®led to compensate for enzyme inactivation maintaining substrate conversion constant. Throughput can be maintained within speci®ed margins of variation by using several reactors operating in parallel but displaced in time. Enzyme inactivation has been usually modeled under non-reactive conditions, leaving aside the effect of substrate and products on enzyme stability. Results are presented for the design of enzyme reactors under the above operational strategy, considering ®rst-order biocatalyst inactivation kinetics modulated by substrate and products. The continuous production of hydrolyzed-isomerized whey permeate with immobilized lactase and glucose isomerase in sequential packed-bed reactors is used as a case study. Kinetic and inactivation parameters for immobilized lactase have been determined by the authors; those for glucose isomerase were taken from the literature. Except for lactose, all other substrates and products were positive modulators of enzyme stability. Reactor design was done by iteration since it depends on enzyme inactivation kinetics. Reactor performance was determined based on a preliminary design considering non-modulated ®rst-order inactivation kinetics and confronted to such pattern. The new pattern of inactivation was then used to redesign the reactor and the process repeated until reactor performance (considering modulation) matched the assumed pattern of inactivation. Convergence was very fast and only two iterations were needed. List of symbolsA m 2 cross sectional area of reactor a kat/kg speci®c activity of catalyst D m reactor diameter d s total operation time for each reactor cycle E kat enzyme activity e kat/m 3 volumetric enzyme activity F m 3 /s total process¯ow rate F 0i m 3 /s initial feed¯ow-rate to each reactor H number of enzyme half-lives used in the reactor H b m catalyst bed height H R m reactor height K eq kg-mole/m 3 equilibrium constant of glucose isomerization to fructose ( V G K F aV F K G ) K F kg-mole/m 3 IGI Michaelis constant for fructose K G kg-mole/m 3 IGI Michaelis constant for glucose K L kg-mole/m 3 CIL Michaelis constant for lactose K P kg-mole/m 3 CIL competitive inhibition constant for galactose k cat catalytic rate constant for lactose hydrolysis k H cat catalytic rate constant for glucose isomerization k D s À1 ®rst-order inactivation rate constant under no modulation k DJ s À1 ®rst-order inactivation rate constant under modulation by J M kg catalyst mass N 1 ± CIL global modulation factor N 2 ± IGI global modulation factor N R ± number of reactors n L ± CIL modulation factor by lactose n P ± CIL modulation factor by galactose n G ± IGI modulation factor by glucose n F ± IGI modulation factor by fructose R F ± ratio of minimum to maximum ow rate s 0 kg-mole/m 3 feed lactose concentration t s time of operation t s s time interval between e...

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Effects of temperature on the hydrolysis of lactose by immobilized β‐galactosidase in a capillary bed reactor

Cited by 26 publications

References 6 publications

Production of Hypoallergenic Antibacterial Peptides from Defatted Soybean Meal by a Membrane Associated Bioreactor: A Bioprocess Engineering Study with Comprehensive Product Characterization

Production of Hypoallergenic Antibacterial Peptides from Defatted Soybean Meal by a Membrane Associated Bioreactor: A Bioprocess Engineering Study with Comprehensive Product Characterization

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

Design of immobilized enzyme reactors for the continuous production of fructose syrup from whey permeate

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