Multistage leaching of metals from spent lithium ion battery waste using electrochemically generated acidic lixiviant.

Lithium ion battery (LIB) waste contains significant valuable resources that could be recovered and reused to manufacture new products. This study aimed to develop an alternative process for extracting metals from LIB waste using acidic solutions generated by electrolysis for leaching. Results showed that solutions generated by electrolysis of 0.5 M NaCl at 8 V with graphite or mixed metal oxide (MMO) electrodes were weakly acidic and leach yields obtained under single stage (batch) leaching were poor (<10%). This was due to the highly acid-consuming nature of the battery waste. Multistage leaching with the graphite electrolyte solution improved leach yields overall, but the electrodes corroded over time. Though yields obtained with both electrolyte leach solutions were low when compared to the 4 M HCl control, there still remains potential to optimise the conditions for the generation of the acidic anolyte solution and the solubilisation of valuable metals from the LIB waste. A preliminary value proposition indicated that the process has the potential to be economically feasible if leach yields can be improved, especially based on the value of recoverable cobalt and lithium.

Kinetic analysis of the slow skeletal myosin MHC-1 isoform from bovine masseter muscle.

Several heavy chain isoforms of class II myosins are found in muscle fibres and show a large variety of different mechanical activities. Fast myosins (myosin heavy chain (MHC)-II-2) contract at higher velocities than slow myosins (MHC-II-1, also known as beta-myosin) and it has been well established that ADP binding to actomyosin is much tighter for MHC-II-1 than for MHC-II-2. Recently, we reported several other differences between MHC-II isoforms 1 and 2 of the rabbit. Isoform II-1 unlike II-2 gave biphasic dissociation of actomyosin by ATP, the ATP-cleavage step was significantly slower for MHC-II-1 and the slow isoforms showed the presence of multiple actomyosin-ADP complexes. These results are in contrast to published data on MHC-II-1 from bovine left ventricle muscle, which was more similar to the fast skeletal isoform. Bovine MHC-II-1 is the predominant isoform expressed in both the ventricular myocardium and slow skeletal muscle fibres such as the masseter and is an important source of reference work for cardiac muscle physiology. This work examines and extends the kinetics of bovine MHC-II-1. We confirm the primary findings from the work on rabbit soleus MHC-II-1. Of significance is that we show that the affinity of ADP for bovine masseter myosin in the absence of actin (represented by the dissociation constant K(D)) is weaker than originally described for bovine cardiac myosin and thus the thermodynamic coupling between ADP and actin binding to myosin is much smaller (K(AD)/K(D) approximately 5 instead of K(AD)/K(D) approximately 50). This may indicate a distinct type of mechanochemical coupling for this group of myosin motors. We also find that the ATP-hydrolysis rate is much slower for bovine MHC-II-1 (19 s(-1)) than reported previously (138 s(-1)). We discuss how this work fits into a broader characterisation of myosin motors from across the myosin family.