Influence of silver nanoparticles on the enhancement and transcriptional changes of glucosinolates and phenolic compounds in genetically transformed root cultures of Brassica rapa ssp. rapa

Bioprocess and Biosystems Engineering - Glucosinolates (GSLs) and phenolic compounds (PCs) are biologically active and involved in the defense reaction of plants; these compounds have a beneficial...     

Non-linear control of continuous bioreactors

Control of bioreactors has achieved importance in the recent years. This may be due to the fact that they are difficult to control which may be attributed to its nonlinear dynamic behavior. The model parameters of the bioreactor also vary in an unpredictable manner. The complexity of the biochemical processes inhibits the accurate modeling and also the lack of suitable sensors make the process state difficult to characterize. Considerable emphasis has been placed on the control of fed-batch fermentors because of their prevalence in industries. However, when production of biomass is to be optimized, continuous operation is desirable. Several procedures are available for the nonlinear control of processes, viz., differential geometric approach, internal model control approach, reference synthesis technique, predictive control design, etc., but the major disadvantage of these approaches is the computational time required to perform the prediction optimization. In this study, a nonlinear controller based on a polynomial discrete time model (NARMAX) is evaluated for its performance on a fermentor. It can be shown that a nonlinear self-tuning controller based on NARMAX model can be extended to the control of fermentors. The response is smooth for both load and setpoint changes even when process parameters are assumed to be zero and uncertainty in parameters are present and in the presence of controller constraints. The control action can be made more or less robust by changing the design parameters appropriately. Therefore, nonlinear self-tuning controller is suitable for control of industrial processes.     

The Catecholaminergic Polymorphic Ventricular Tachycardia Mutation R33Q Disrupts the N-terminal Structural Motif That Regulates Reversible Calsequestrin Polymerization

Calsequestrin undergoes dynamic polymerization with increasing calcium concentration by front-to-front dimerization and back-to-back packing, forming wire-shaped structures. A recent finding that point mutation R33Q leads to lethal catecholaminergic polymorphic ventricular tachycardia (CPVT) implies a crucial role for the N terminus. In this study, we demonstrate that this mutation resides in a highly conserved alternately charged residue cluster (DGKDR; cluster 1) in the N-terminal end of calsequestrin. We further show that this cluster configures itself as a ring system and that the dipolar arrangement within the cluster brings about a critical conformational flip of Lys³¹-Asp³² essential for dimer stabilization by formation of a H-bond network. We additionally show that Ca²⁺-induced calsequestrin aggregation is nonlinear and reversible and can regain the native conformation by Ca²⁺ chelation with EGTA. This study suggests that cluster 1 works as a molecular switch and governs the bidirectional transition between the CASQ2 monomer and dimer. We further demonstrate that mutations disrupting the alternating charge pattern of the cluster, including R33Q, impair Ca²⁺-CASQ2 interaction, leading to altered polymerization-depolymerization dynamics. This study provides new mechanistic insight into the functional effects of the R33Q mutation and its potential role in CPVT.