Suitability of sodium lactate as cryoprotectant and its effect on gel forming ability and protein denaturation of croaker fish surimi during frozen storage

The effect of sodium lactate is compared with sucrose + sorbitol + sodium tri-poly phosphate as cryoprotectant on gel forming ability & protein denaturation of croaker surimi during frozen storage at -20±2°C for 90 days was evaluated. The quality of Croaker surimi with 6% (w/v) sodium lactate was examined in terms of biochemical parameters of muscle protein, thaw drip, gel strength and calcium ATPase activity :.omparing with those of surimi added with sucrose/sorbitol & without additive as control. Both the cryoprotectants minimized the negative effects of frozen storage on physico-chemical traits of myofibrillar proteins which was evident from the biochemical and sensory parameters. The residual Ca2+ ATPase activity and gel strength of surimi with sodium lactate were higher than those of control throughout 90 days of storage. Ca2+ A TPase activity and gel strength found a high positive correlation. From the results, it was found that sodium lactate was equally effective in preservation of croaker muscle protein native structure during frozen storage as the sucrose/ sorbitol and also less sweet without any risk of maillard browning.

Synthesis and surface morphology of tetraaniline-block-poly(L-lactate) diblock oligomers

Tetraaniline-block-poly(L-lactide) diblock oligomers are synthesized via ring-opening polymerization. The diblock oligomers cast from all L-lactide selective solvent (chloroform) show spherical aggregates for the leucoemeraldine state, and ring-like structures that are composed of much smaller spherical aggregates for the emeraldine state. The formation mechanisms of the two different surface morphologies are discussed in detail.

Effects of rare earth ions and calmodulin on the activity of lactate dehydrogenase

In this paper, the effects of rare earth ions (La3+, Eu3+, Dy3+, Yb3+) and their complexes with calmodulin on the activity of lactate dehydrogenase (LDH) were investigated. The results reveal that whether binding with calmodulin or not, rare earth ions show a minor activation effects on LDH when their concentrations are less than 3 mu mol (.) L-1, but indicate some strong inhibitory effects on LDH activity when the concentrations are above 5 mu mol (.) L-1. Calmodulin, which is a calcium-dependent regulator, can stimulate LDH activity and release the inhibitory effects of rare earth ion. Diethylenetriamine pentaacetic acid(DTPA) and its derivatives bisdimethylamide-diethylenetriamine pentaacetic acid (DTPA-BDMA), bisisonicotinyl-diethylenetriamine pentaacetic acid (DTPA-BIN), which are often used as ligands to metal ions, inhibit LDH activity when their concentrations are above 5 mu mol (.) L-1. Calmodulin can also release their inhibitory effects at the same time.

Comparison of the Lactate Pro and Analox GM7 blood lactate analysers

van Someren KA, Howatson G, Nunan D, Thatcher R, Shave R., Comparison of the Lactate Pro and Analox GM7 blood lactate analysers, Int J Sports Med. 2005 Oct;26(8):657-61. RAE2008

Stereocomplexes Formed From Select Oligomers of Polymer d-lactic Acid (PDLA) and l-lactate May Inhibit Growth of Cancer Cells and Help Diagnose Aggressive Cancers-Applications of the Warburg Effect.

It is proposed that select oligomers of polymer d-lactic acid (PDLA) will form a stereocomplex with l-lactate in vivo, producing lactate deficiency in tumor cells. Those cancer cells that utilize transport of lactate to maintain electrical neutrality may cease to multiply or die because of lactate trapping, and those cancer cells that benefit from utilization of extracellular lactate may be impaired. Intracellular trapping of lactate produces a different physiology than inhibition of LDH because the cell loses the option of shuttling pyruvate to an alternative pathway to produce an anion. Conjugated with stains or fluorescent probes, PDLA oligomers may be an agent for the diagnosis of tissue lactate and possibly cell differentiation in biopsy specimens. Preliminary experimental evidence is presented confirming that PDLA in high concentrations is cytotoxic and that l-lactate forms a presumed stereocomplex with PDLA. Future work should be directed at isolation of biologically active oligomers of PDLA.