The aim of the present work was to study the influence of multiple bioprocess parameters for the maximum production of lipase from Pseudomonas sp. (1 %, w/v), peptone (3 %, w/v) and KCl (0.05 %, w/v)
Herein, we report the drying kinetics behavior of tempered lentil seeds (CDC Maxim variety) by utilizing a microwave-assisted infrared thermal method and thereby presenting a successful mathematical model for it. The drying characteristics of lentils using thin-layer microwave drying with and without hot air predrying were evaluated in a laboratory scale microwave dryer. The drying experiments were carried out at 300 and 750 W, and the predrying experiment was performed at room temperature (23 C).Out of several thin-layer mathematical models evaluated with the experimental data, Page model has been found the most appropriate model to predict drying process of lentils with high value of coefficient of determination (0.995), low values of chi-square (0.0012), root mean square error (0.0343), and mean relative percentage error (4.9997).Further, the influence of bioyield force and changes in the particle density of processed seeds have also been evaluated in the present study. The results showed that combination of low infrared power (0.375 kW) to the different microwave power levels led to a significant reduction of drying time. The results also showed that processing of lentil seeds significantly reduces the bioyield force of raw seeds, providing less firmness to the product and thereby shortening the cooking time. The above findings can facilitate the design and operation of infrared-assisted microwave drying of other legumes.
K E Y W O R D Sdrying process, infrared, lentils, mathematical model, microwave
A dual-enzyme
metal–organic hybrid crystal was constructed
through self-assembling of manganese phosphate embedded with β-galactosidase
and L-arabinose isomerase for facile synthesis of rare sugar D-tagatose.
The synthesized crystal-like hierarchical system (MnHC@β-Gal+L-AI)
was extensively characterized for structural features and catalytic
reactions. The results indicated that upon immobilization onto the
hybrid crystal, the activity of β-galactosidase and L-arabinose
iomerase was enhanced by a factor of 1.6- and 1.5-fold, respectively.
The developed MnHC@β-Gal+L-AI exhibited excellent efficiency
with a net equilibrium level conversion of low-cost substrate whey
lactose (100%) into D-glucose (∼50%), D-galactose (∼25%),
and D-tagatose (∼25%). In addition, the fabricated hybrid crystals
displayed cofactor regeneration ability. Therefore, the developed
hybrid system was observed to be efficiently reused more than 5 times
in a batch level conversion. Hence, the developed dual-enzyme-based
hybrid crystal provides a platform for direct transformation of whey
lactose into rare sugar D-tagatose.
Catalase from a thermophilic bacterium belonging to the genus Geobacillus was purified and covalently immobilized onto a functionalized polymer via a spacer with an objective to improve its kinetic and biochemical properties. This is the first report on the purification and immobilization of catalase from the genus Geobacillus. The tetrameric catalase of about 221 kDa was successfully purified using a multistep purification strategy. A shift in pH and temperature optima from 8.0 to 9.0 and 55 C to 60 C, respectively was recorded after covalent binding of catalase onto the functionalized matrix. The kinetic constants i.e. K m , V max , K cat and K cat /K m were found to be 1.2 mM, 4.43 Â 10 6 IU, 6.3 Â 10 5 s À1 and 5.25 Â 10 8 s À1 M À1 for free, and 1.8 mM, 4.01 Â 10 6 IU, 5.9 Â 10 5 s À1 and 3.20 Â 10 8 s À1 M À1 for immobilized catalase, respectively. The ease of binding of alkalothermophilic catalase from a novel isolated bacterium G. extremocatsoochus sp. nov., MTCC 5873 onto a low cost activated cellulose support demonstrated enhanced pH and thermal stability as compared to its free counterpart. This immobilized catalase preparation with improved characteristics has good potential for diverse applications. The present findings provide valuable information on how to tailor enzymes and supported polymer matrices to improve the performance of a biocatalyst.
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