A research note: Effect of Hofmeister salts on meat iridescence in cooked pork

The effect of Hofmeister salts (NaCl, NaSCN, Na2SO4, KCl, LiCl, CaCl2) on surface iridescence in cooked pork was investigated. Strongest iridescence occurred in samples treated with NaSCN, NaCl and KCl. Control samples and LiCl, CaCl2 and Na2SO4 treatments showed weaker iridescence. However, differences between KCl and LiCl, CaCl2 and Na2SO4 were not statistically significant (p > 0.05). Nevertheless, a tendency of chaotropic salts (NaSCN, NaCl, KCl) to cause stronger iridescence was noted that might be explained with a more effective solubilization of myofibrillar proteins (MPs), reducing incoherent scattering from the myofibrils and thus enhancing multilayer interference.

Spatial and temporal requirement of Mlp60A isoforms during muscle development and function in Drosophila melanogaster

Many myofibrillar proteins undergo isoform switching in a spatio-temporal manner during muscle development. The biological significance of the variants of several of these myofibrillar proteins remains elusive. One such myofibrillar protein, the Muscle LIM Protein (MLP), is a vital component of the Z-discs. In this paper, we show that one of the Drosophila MLP encoding genes, Mlp60A, gives rise to two isoforms: a short (279 bp, 10 kDa) and a long (1461 bp, 54 kDa) one. The short isoform is expressed throughout development, but the long isoform is adult-specific, being the dominant of the two isoforms in the indirect flight muscles (IFMs). A concomitant, muscle-specific knockdown of both isoforms leads to late pupal lethality, with the surviving flies being majorly flight defective. Mlp60A null flies show developmental lethality, and muscle defects in the individuals surviving till the third instar larval stage. This lethality could be rescued partially by muscle-specific overexpression of the short isoform. Almost 90% of the long isoform-specific P-element insertion mutant flies show a compromised flight ability and have reduced sarcomere length. Hence, our data shows that the two Mlp60A isoforms are functionally specialized, to ensuring normal embryonic muscle development and adult flight muscle function.

Role of Ovalbumin/β-Cyclodextrin in Improving Structural and Gelling Properties of Culter alburnus Myofibrillar Proteins during Frozen Storage

This study aimed to analyze the cryoprotective effect of a ovalbumin (OVA) and β-cyclodextrin (βCD) mixture (3:1, OVA/βCD) on the structure, rheology and gelling properties of myofibrillar proteins (MPs) during 90 days of frozen storage. A mixture of OVA/βCD at different concentrations (0, 2, 4, and 6%) was added to MPs and stored at −18 °C for 90 days. The addition of OVA/βCD significantly decreased the sulfhydryl contents while it increased the surface hydrophobicity, which was closely connected with tertiary structural changes. Circular dichroism analysis showed that the addition of OVA/βCD enhanced the stability of the secondary structure by inhibiting the decline in the α-helix. Rheological properties analysis indicated that 6% OVA/βCD treatment showed better storage modulus (G’) and loss modulus (G”). In addition, treatment of OVA/βCD showed better gel forming properties than the control group (0%), helping to form a homogeneous and denser gel network. The results proved that 6% OVA/βCD could be act as a promising cryoprotectant, which can improve the structure and gel behavior of Culter alburnus MPs during frozen storage. Moreover, OVA/βCD could be a potential alternative to conventional cryoprotectants at the industrial level to increase the economic and commercial values of seafood products.