Marutomo Co.

Iyo, Japan

Marutomo Co.

Iyo, Japan

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Morishige H.,Ehime University | Sugahara T.,Ehime University | Nishimoto S.,Ehime University | Muranaka A.,Ehime University | And 3 more authors.
Cytotechnology | Year: 2011

We focused on the biological activity of the collagen extracts obtained from the giant edible jellyfish, Nemopilema nomurai. Jellyfish collagen extracts stimulates the production of immunoglobulins (Igs) and cytokines by human hybridoma cells and human peripheral blood lymphocytes. Therefore, we examined the immunoregulatory function of jellyfish collagen extracts in mice. Intake of jellyfish collagen extracts facilitated the Ig production activity of lymphocytes from spleen and Peyer's patch. Furthermore, the levels of Igs in the serum clearly increased after the administration of jellyfish collagen extracts. Intake of bovine collagen from Achilles' tendon also activated lymphocytes activity in mice. The activity of total and antigen-specific Ig production in splenocytes from OVA-challenged mice was also enhanced by collagen intake. However, the total and OVA-specific IgE levels in the serum were not affected by the collagen intake. These results suggested that jellyfish collagen extracts stimulates an immune response in vivo, without inducing allergic complications. © Springer Science+Business Media B.V. 2011.


Doi M.,Marutomo Co.
Sensors and Materials | Year: 2011

It is difficult to describe the Katsuobushi (dried bonito) taste, especially that of Karebushi (molded died bonito), because it contains heartiness (kokumi) taste. Therefore, there is no study on the taste oiKarebushi. In this study, we revealed the kokumi taste of Karebushi and other Japanese soup stock materials using a taste sensor.


Putra A.B.N.,Ehime University | Nishi K.,Ehime University | Shiraishi R.,Marutomo Co. | Doi M.,Marutomo Co. | Sugahara T.,Ehime University
Molecular Immunology | Year: 2014

We previously reported that jellyfish collagen stimulates both the acquired and innate immune responses. In the acquired immune response, jellyfish collagen enhanced immunoglobulin production by lymphocytes in vitro and in vivo. Meanwhile, in the innate immune response jellyfish collagen promoted cytokine production and phagocytotic activity of macrophages. The facts that jellyfish collagen plays several potential roles in stimulating cytokine production by macrophages have further attracted us to uncover its mechanisms. We herein describe that the cytokine production-stimulating activity of jellyfish collagen was canceled by a Toll-like receptor 4 (TLR4) inhibitor. Moreover, jellyfish collagen stimulated phosphorylation of inhibitor of κBα (IκBα), promoted the translocation of nucleus factor-κB (NF-κB), and activated c-Jun N-terminal kinase (JNK). A JNK inhibitor also abrogated the cytokine production-stimulating activity of jellyfish collagen. These results suggest that jellyfish collagen may facilitate cytokine production by macrophages through activation of NF-κB and JNK via the TLR4 signaling pathways. © 2013 Elsevier Ltd.


Putra A.B.N.,Ehime University | Nishi K.,Ehime University | Shiraishi R.,Marutomo Co. | Doi M.,Marutomo Co. | Sugahara T.,Ehime University
Journal of Functional Foods | Year: 2015

Jellyfish collagen, extracted from Nemopilema nomurai, was found to stimulate murine macrophage-like J774.1 cells. However, few reports have determined the immunostimulatory effects of jellyfish collagen on the innate immune response. We herein demonstrate the effect of jellyfish collagen on mouse bone marrow-derived dendritic cells (BMDCs). Jellyfish collagen stimulated TNF-α, IL-6, IL-1β and IL-12 production by BMDCs as the result of the elevation of gene expression level of these cytokines. In addition, jellyfish collagen-treated BMDCs have more wrinkles and longer pseudopodia on the cell surface compared with the control cells. Jellyfish collagen also stimulated cell-surface MHC-II expression level. Furthermore, jellyfish collagen downregulated phagocytosis capacity of BMDCs. Thus, our findings suggest that JC has the potential to activate DCs and thereby contribute to health promotion. © 2015 Elsevier Ltd.


Putra A.B.N.,Ehime University | Morishige H.,Ehime University | Nishimoto S.,Ehime University | Nishi K.,Ehime University | And 3 more authors.
Journal of Functional Foods | Year: 2012

As we previously reported, jellyfish collagen stimulates immunoglobulin and cytokine productions by lymphocytes . in vitro and . in vivo. Herein, the effects of collagens from jellyfish and bovine Achilles tendon on the innate immune response, especially on the activity of macrophages were evaluated. Macrophage functions were examined by the phagocytotic activity, cytokine production activity, and gene expression. The phagocytosis of the mouse J774.1 cells was enhanced by both collagens. Collagens from jellyfish and bovine Achilles tendon also stimulated the productions of tumor necrosis factor-α and interleukin-6 by J774.1 cells and mouse primary peritoneal macrophages as the result of elevated gene expression levels of these cytokines. Oral administration of collagens elevated cytokine production by peritoneal macrophages in mice. On the contrary, collagens suppressed gene expression of PPARγ1 in macrophages. It is supposed from this result that collagens may stimulate the cytokine production by suppressing the PPARγ1 expression. Collagens from jellyfish and bovine Achilles tendon enhanced not only the acquired immune response but also the innate immune response through the activation of macrophages. © 2012 Elsevier Ltd.


Takenaka S.,Kobe University | Umeda M.,Kobe University | Senba H.,Kobe University | Koyama D.,Marutomo Co. | And 3 more authors.
Journal of the Science of Food and Agriculture | Year: 2016

BACKGROUND: Aspergillus repens strain MK82 produces an aspartic protease (PepA_MK82) that efficiently decolorises red-pigmented proteins during dried bonito fermentation. However, further expansion of the industrial applications of PepA_MK82 requires the high-level production and efficient preparation of the recombinant enzyme. RESULTS: The genomic DNA and cDNA fragments encoding the protease were cloned from strain MK82 and sequenced. Phylogenetic analysis of PepA_MK82 and comparisons with previously reported fungal aspartic proteases showed that PepA_MK 82 clusters with different groups of these enzymes. Heterologous expression of PepA_MK82 in Pichia pastoris yielded preparations of higher purity than obtained with an Escherichia coli expression system. Total protease activity in a 100-mL culture of the P. pastoris transformant was 14 times higher than that from an equivalent culture of A. repense MK82. The recombinant PepA_MK82 was easily obtained via acetone precipitation; the final recovery was 83%. PepA_MK82 and its recombinant had similar characteristics in terms of their optimal pH, thermostability, and decolorisation activity. The recombinant was also able to decolorise flaked, dried bonito and to bleach a blood-stained cloth. CONCLUSION: Given its ability to hydrolyse and decolorise red-pigmented proteins, recombinant PepA_MK8 can be exploited in the food industry and as a stain-removal agent in laundry applications. © 2016 Society of Chemical Industry.


Aoki K.,Sagami Women's University | Matsubara S.,Kobe University | Umeda M.,Kobe University | Tachibanac S.,Marutomo Co. | And 2 more authors.
Journal of the Science of Food and Agriculture | Year: 2013

Background: Katsuobushi is a dried, smoked and fermented bonito used in Japanese cuisine. During the fermentation process with several Aspergillus species, the colour of Katsuobushi gradually changes from a dark reddish-brown derived from haem proteins to pale pink. The change in colour gives Katsuobushi a higher ranking and price. This study aimed to elucidate the mechanism of decolourisation of Katsuobushi. Results: A decolourising factor from the culture supernatant of Aspergillus (Eurotium) repens strain MK82 was purified to homogeneity. The purification was monitored by measuring the decolourising activity using equine myoglobin and bovine haemoglobin as substrates. It was found that the decolourising factor had protease activity towards myoglobin and haemoglobin. Complete inhibition of the enzyme by the inhibitor pepstatin A and the internal amino acid sequence classified the protein as an aspartic protease. The enzyme limitedly hydrolysed myoglobin between 1-Met and 2-Gly, 43-Lys and 44-Phe, and 70-Leu and 71-Thr. The purified enzyme decolourised blood of Katsuwonus pelamis (bonito) and a slice of dried bonito. Conclusion: It is proposed that aspartic protease plays a role in the decolourisation of Katsuobushi by the hydrolysis of haem proteins that allows the released haem to aggregate in the dried bonito. © 2012 Society of Chemical Industry.


PubMed | Ehime University and Marutomo Co.
Type: Journal Article | Journal: Molecular immunology | Year: 2014

We previously reported that jellyfish collagen stimulates both the acquired and innate immune responses. In the acquired immune response, jellyfish collagen enhanced immunoglobulin production by lymphocytes in vitro and in vivo. Meanwhile, in the innate immune response jellyfish collagen promoted cytokine production and phagocytotic activity of macrophages. The facts that jellyfish collagen plays several potential roles in stimulating cytokine production by macrophages have further attracted us to uncover its mechanisms. We herein describe that the cytokine production-stimulating activity of jellyfish collagen was canceled by a Toll-like receptor 4 (TLR4) inhibitor. Moreover, jellyfish collagen stimulated phosphorylation of inhibitor of B (IB), promoted the translocation of nucleus factor-B (NF-B), and activated c-Jun N-terminal kinase (JNK). A JNK inhibitor also abrogated the cytokine production-stimulating activity of jellyfish collagen. These results suggest that jellyfish collagen may facilitate cytokine production by macrophages through activation of NF-B and JNK via the TLR4 signaling pathways.

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