Publishing type：Research paper (scientific journal)   Publisher：Japan Poultry Science Association  

DOI： 10.2141/jpsa.0200032

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Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s13197-020-04391-9

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Other Link： http://link.springer.com/article/10.1007/s13197-020-04391-9/fulltext.html

Language：Japanese   Publishing type：Research paper (scientific journal)  

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Language：English   Publisher：Japanese Society of Food Chemistry  

Olive leaf (<i>Olea europaea</i> L.) is an underutilized resource of olive tree but has a high polyphenol content, so it has the potential to be used as a food ingredient. In this study, we investigated the effects of olive leaf water extracts on the physical properties of chicken breast sausage (CBS). Olive leaf water extracts were prepared at 4 (OEx₄) and 80°C (OEx₈₀) from dried olive leaf powder and they were applied to CBS preparation within the concentration range 0.05 to 0.5% (w/w minced meat). OEx₄ had 32% lower polyphenol content than OEx₈₀. Water content, expressible water, breaking strength, and viscoelastic properties of CBS with OEx₄ and OEx₈₀ were measured. The analyses of the sausage physical properties showed that adding 0.1% OEx₄ increased the breaking stress (115%), breaking strain (68%), modulus of elasticity (20%), coefficient of viscosity (23%), and water-holding capacity (9%), and the enhancement effects of OEx₄ were much greater than those of OEx₈₀. The gel network of OEx₄-containing CBSs observed by scanning electron microscopy was finer and denser than that of the control CBS. Chemical analyses of the meat proteins showed that OEx₄ induces polymerization of myofibril proteins, especially myosin, via non-disulfide covalent bridges formed between amino and/ or thiol groups. These results indicate that the application of OEx₄ improves the sausage gel properties by inducing non-disulfide-type protein polymerization. This study supports the feasibility of OEx₄ as a new ingredient to improve the texture of gel products prepared from chicken breast minced meat.

DOI： 10.18891/jjfcs.27.1_10

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Language：Japanese   Publisher：The Japanese Society of Fisheries Science  

<p> Yellowtail <i>Seriola quinqueradiata</i> raised on a diet supplemented with 2% olive leaf powder (OLP) was subjected to an analysis of the breaking properties of ordinary muscle. The force-strain curve showed that the slope of the OLP-diet fish curve was higher than that of control-diet fish that were raised on a diet without OLP. There was no significant difference in breaking force value, while the breaking strain value of OLP-diet fish muscle was 24% lower than that of the muscle of control-diet fish. Chemical analysis showed that collagen content was 22% higher in OLP-diet fish than in control-diet fish. These results suggest that the difference in collagen content is the cause of the difference in textural property between OLP-diet fish and control-diet fish. The breaking force of the muscles refrigerated for 3 days was 40% higher in OLP-diet fish than in control-diet fish, suggesting that muscle softening of OLP-diet fish was slower than that of control-diet fish. Electron microscopic observation of the muscles refrigerated for 3 days showed that OLP-diet fish had a more robust endomysium structure than control-diet fish. The present study suggests that the ordinary muscle of OLP-diet fish is high quality in terms of textural property.</p>

DOI： 10.2331/suisan.20-00025

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

Ovalbumin-related protein X (OVAX) is a 50 kDa egg-white protein which has heparin-binding affinity. In this study, migration of OVAX and its heparin-binding performance during embryogenesis of fertilized egg were investigated to explore a possible involvement in chick embryo development. Western blotting of egg yolks at different stages using an anti-OVAX antibody showed that OVAX accumulates in yolk during incubation of fertilized egg. Immunohistochemical analysis of embryo resided in 10-day-incubated eggs showed that OVAX existed in almost all tissues of the embryo. These suggest that OVAX is incorporated from egg white into the embryo through yolk sac. Heparin-sepharose chromatography, isothermal titrating calorimetry using fondaparinux as a ligand, and zeta potential measurement indicated that OVAX retained the heparin-binding affinity (Kd = 0.185 ± 0.037) even after 10 D incubation of fertilized egg, although the affinity was slightly decreased during egg incubation because of acidification of molecular surface charge. In conclusion, although heparin-binding ability of egg-white OVAX slightly decreases during embryogenesis, OVAX incorporated into embryo can retain heparin-binding affinity. Our findings provide a new insight that OVAX participates in the functions of heparin during embryogenesis.

DOI： 10.3382/ps/pez335

PubMed

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Language：English   Publishing type：Research paper (scientific journal)  

Heterozygous missense mutations in several genes in the WNT5A signaling pathway cause autosomal dominant Robinow syndrome 1 (DRS1). Our objective was to clarify the functional impact of a missense mutation in WNT5A on the skeleton, one of the main affected tissues in RS. We delivered avian replication competent retroviruses (RCAS) containing human wild-type WNT5A (wtWNT5A), WNT5AC83S variant or GFP/AlkPO4 control genes to the chicken embryo limb. Strikingly, WNT5AC83S consistently caused a delay in ossification and bones were more than 50% shorter and 200% wider than controls. In contrast, bone dimensions in wtWNT5A limbs were slightly affected (20% shorter, 25% wider) but ossification occurred on schedule. The dysmorphology of bones was established during cartilage differentiation. Instead of stereotypical stacking of chondrocytes, the WNT5AC83S-infected cartilage was composed of randomly oriented chondrocytes and that had diffuse, rather than concentrated Prickle staining, both signs of disrupted planar cell polarity (PCP) mechanisms. Biochemical assays revealed that C83S variant was able to activate the Jun N-terminal kinase-PCP pathway similar to wtWNT5A; however, the activity of the variant ligand was influenced by receptor availability. Unexpectedly, the C83S change caused a reduction in the amount of protein being synthesized and secreted, compared to wtWNT5A. Thus, in the chicken and human, RS phenotypes are produced from the C83S mutation, even though the variant protein is less abundant than wtWNT5A. We conclude the variant protein has dominant-negative effects on chondrogenesis leading to limb abnormalities.

DOI： 10.1093/hmg/ddz071

PubMed

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Language：English   Publishing type：Research paper (scientific journal)  

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Language：English   Publishing type：Research paper (scientific journal)  

Olive leaf is known to have the high polyphenol content of 6-9% in dry weight. We investigated the effects of olive leaf powder (OLP) supplemented to fish feed on muscle protein of red sea bream (Pagrus major). Fish reared with feed containing 8% OLP for 40 days had 1.4 times higher myofibril content and 2.2 times higher acid-soluble collagen content than fish reared with control feed for the same period. On the other hand, sarcoplasmic protein content and collagenase activity of the muscle were almost the same between the control fish and OLP-diet fish. Microstructure observation of fish muscle showed that OLP-diet fish has more rigid endomysium structure than that of the control-diet fish. Since collagen fiber in endomysium is responsible for the texture of the muscle, feeding OLP to aquaculture fish will lead to a harder muscle texture. The present study suggests that OLP is a useful feed additive to enhance the texture of aquaculture red sea bream muscle through strengthening of the collagen structure in the muscle.

DOI： 10.1007/s10695-018-0521-1

PubMed

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

Chicken egg white protein ovalbumin (OVA) undergoes a conversion to a more thermostable form by alkali treatment, which is assumed to be involved in the physiological functions of OVA. Ovalbumin-related protein X (OVAX), a chicken egg white protein, has 77% sequence similarity to OVA and binds to heparin. In this study, structure characteristics and heparin-binding affinity of alkali-treated OVAX were investigated. Cation-exchange chromatography using SP Sepharose resin showed that alkali treatment (pH 10, 55°C) of OVAX induces the occurrence of a distinct OVAX form with a less positive-charge (acidic OVAX). Circular dichroism and tryptophan-fluorescence analyses showed that the newly-formed acidic OVAX form has an 8% lower α-helical content than its native counterpart, while there is no significant difference in steric environments around tryptophan residues between the 2 forms. The OVAX structure built by homology-modeling showed that OVAX possess a basic cluster domain with α-helix equivalent to 7% of total secondary structures, which does not contain any tryptophan residues. These results suggest that, during alkali treatment, OVAX undergoes mainly a conformational change of the α-helical basic cluster domain and thereby forms acidic OVAX. Acidic OVAX induced by alkali treatment exhibited weaker interactions with Heparin Sepharose resin than native OVAX did. Our results suggest that OVAX basic cluster domain is likely a specific binding site of heparin. Consequently, it is suggested that alkali treatment causes the collapse of the OVAX heparin binding site, which might participate in regulating the functions of heparin.

DOI： 10.3382/ps/pey024

PubMed

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