2.6. Droplet Polymerization and Spore GerminationThe droplets were generated using the microfluidic device with a flow-focusing merely technique. The dispersive phase (DP) consisted of the mixture of potassium persulphate (initiator, 0.19 wt%), D-sorbitol (cross-linker, 0.6 wt%), PBS solution (56 wt%), NIPAM (24.8 wt%) and BT spores and LB broth (0.18 wt%). The continuous phase (CP) is the mixture solution of G-oil and Abil EM90 (2 wt%). The microdroplet generation in the microfluidic device was observed using an optical microscope with a charge-coupled-device camera (Elipse Ti-S, Nikon, Tokyo, Japan). Once the microdroplets were generated through flow-focusing, the microdroplets were collected and suspended in TEMED/G-oil mixture (7.7 vol%) for the polymerization.
TEMED is acted as a catalyst for encouraging the polymerization and produce hydrogel microcapsules. In addition, the Abil-EM90 was use
In recent years, various types of biosensors have been increasingly becoming practical and useful tools in a wide variety of analytical devices [1,2]. The immobilization of biological elements to realize the biosensor is an essential step for the successful construction of a diagnostic system. In order to allow the detection of a small amount of target sample and improve detection performance, bioreceptor proteins must be immobilized onto biosensor chip surfaces with high density and nonspecific adsorption avoided or at least minimized. Moreover, orientation control with retention of protein conformation and activity is a required task to be established [3].
One method involves the Brefeldin_A physical adsorption via van der Waals forces, ionic binding or hydrophobic and polar forces Navitoclax mw on an insoluble matrix. This is a simple process which causes little disruption of the proteins, while it is unstable during the binding procedure due to the highly dependency against environmental conditions in maintaining its functional characteristics. Thus, the resulting receptor layer seems to form heterogeneous and random orientation. Another method can also be constructed by crosslinking functional reagents by a certain number of functional groups due to its simple procedure and strong chemical bond of proteins. This is widely used for stabilization of proteins that are covalently bound onto the support platform generated by chemical treatment. However, this method has also disadvantages as follows: the difficulty in controlling the crosslinking reaction, the gelatinous nature of the proteins and the relatively low activity of the proteins due to the specific structural features [3,4].