Moriya, Japan
Moriya, Japan

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Patent
Itoham Foods Inc., Hosoda Kogyo Co. and MAYEKAWA Manufacturing CO. | Date: 2011-01-24

A foreign matter removal device 10 preliminary cleans the work 50 in a bucket 12 housed in an input tank 15, then further cleans the work 50 in buckets 13, 14 housed in cleaning tanks 16, 17 by agitating cleaning liquid while inverting the buckets to transfer the work to a subsequent bucket. Particularly, the bottom of the cleaning tank is formed such that the nearer to a center of the bottom, the deeper the bottom becomes. The cleaning liquid overflowing from the cleaning tanks are stored in auxiliary tanks 22, 23. First and second ejection units 29a, 29b are arranged at different heights in the cleaning tank to generate a circulating flow in the cleaning liquid.


Mio K.,Japan National Institute of Advanced Industrial Science and Technology | Mio M.,Japan National Institute of Advanced Industrial Science and Technology | Arisaka F.,Tokyo Institute of Technology | Sato M.,Itoham Foods Inc. | Sato C.,Japan National Institute of Advanced Industrial Science and Technology
Progress in Biophysics and Molecular Biology | Year: 2010

The NaChBac is a prokaryotic homologue of the voltage-gated sodium channel found in the genome of the alkalophilic bacterium Bacillus halodurans C-125. Like a repeating cassette of mammalian sodium channel, the NaChBac possesses hydrophobic domains corresponding to six putative transmembrane segments and a pore loop, and exerts channel function by forming a tetramer although detailed mechanisms of subunit assembly remain unclear. We generated truncated mutants from NaChBac, and investigated their ability to form tetramers in relation to their channel functions. A mutant that deletes almost all of the C-terminal coiled-coil structure lost its voltage-dependent ion permeability, although it was properly translocated to the cell surface. The mutant protein was purified as a tetramer using a reduced concentration of detergent, but the association between the subunits was shown to be much weaker than the wild type. The chemical cross-linking, blue native PAGE, sedimentation velocity experiments, size exclusion chromatography, immunoprecipitation, and electron microscopy all supported its tetrameric assembly. We further purified the C-terminal cytoplasmic domain alone and confirmed its self-oligomerization. These data suggest that the C-terminal coiled-coil structure stabilizes subunit-to-subunit interactions of NaChBac, but is not critical for their tetramer formation. © 2010 Elsevier Ltd.


Sakamoto T.,Ibaraki University | Sasaki S.,Ibaraki University | Nakade K.,Itoham Foods Inc. | Ichinoseki S.,Itoham Foods Inc. | And 2 more authors.
Food Science and Technology Research | Year: 2013

Previously, it was clarified that myofibril gelation was enhanced by the basic protein glyceraldehyde 3-phosphate dehydrogenase (GPD). In this study, the mechanism of the gel-enhancing action of GPD to myosin B was evaluated through the study of the surface properties of GPD. GPD and myosin B were prepared from pork loin. Succinylated GPD (S-GPD) was successfully prepared without any loss of solubility at a weight ratio (succinic anhydrate to GPD) of 1.0. Though gelation of myosin B alone required a minimum protein concentration of 4.0% (w/v), the addition of GPD enhanced the gelation of myosin B at a concentration of 3.5% (w/v). Furthermore, GPD increased the gel strength drastically at concentrations above 4.5% (w/v). On the other hand, the addition of S-GPD did not improve the gelling property of myosin B. SDS-PAGE showed molecular interaction between GPD and myosin B, but not between S-GPD and myosin B. However, in the case of GPD, the GPD band became insoluble under coexistence of GPD with myosin B. Meanwhile, the myosin heavy chain was partially soluble. Furthermore, actin and GPD bands became thicker in the insoluble fraction after mixing of G-actin and GPD. These results indicate that positive charges on the surface of GPD are necessary to enhance the gelation of myosin B.


Nodake K.,Itoham Foods Inc.
Animal science journal = Nihon chikusan Gakkaihō | Year: 2013

The purpose of this study was to assess an evaluation method using an artificial taste sensor, in comparison with chemical analysis and sensory evaluation of the taste of meat during curing. Samples of Canadian pork were treated with salt, nitrite and phosphate. Curing time ranged from 0 to 168 h. In the sensory evaluation, there were no significant differences in the all characteristic items at 72-h cured sample compared to the 0-h sample. Some of the characteristic items for the 168-h sample (umami, overall taste, richness and overall palatability) showed significant difference (P < 0.05) compared to the 0-h sample. Taste sensor analysis indicated that the sensor outputs of bitterness and saltiness were significantly correlated with curing time (R = 0.98 and 0.97, respectively), and total free amino acids (R = 0.91 and 0.96, respectively). The sensor output of bitterness was significantly correlated (R = 0.96) with the sum of amino acids corresponding to bitter taste. The increase in the chemical components contributing to bitterness and/or saltiness was indicated as the cause of the characteristic taste. Taste sensor analysis may be applicable as a qualitative method for evaluating taste characteristics generated during the curing of manufactured cooked meat products. © 2013 Japanese Society of Animal Science.


Miyaguchi Y.,Ibaraki University | Sakamoto T.,Ibaraki University | Sasaki S.,Ibaraki University | Nakade K.,Itoham Foods Inc. | And 4 more authors.
Animal Science Journal | Year: 2011

Porcine glycoliytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (G3PD) was prepared effectively by a combination of ethylene diamine tetra-acetate (EDTA) pretreatment and affinity purification. After salting out of porcine sarcoplasmic proteins (SP) with ammonium sulfate at 75% saturation, the obtained supernatant (SP-f3) was treated with EDTA, leaving G3PD in the supernatant (G3PD-E) and most other SPs in the precipitate. At that time, the separation of G3PD-E required more than 20mmol/L EDTA. G3PD-E was then subjected to affinity purification by batchwise method using blue-sepharose CL-6B, and purified G3PD (G3PD-AP) was obtained using 2mol/L potassium chloride (KCl) as an eluent. Texture analysis showed that the hardness, adhesiveness and gumminess of the myofibril gel at 0.2-mol/L NaCl increased with the addition of G3PD-AP. Scanning electron microscopy revealed that the G3PD-AP reinforced the gel network of the myofibril. However, scanning electron micrograph analysis showed that the network-structure of the gel by the addition of G3PD-AP developed in a different manner from that by adding 0.6mol/L NaCl. These results showed that glycolytic enzyme, G3PD, contributes to the improvement of the rheological properties of meat products. © 2010 The Authors. Journal compilation © 2010 Japanese Society of Animal Science.


Sasaki S.,Ibaraki University | Ogawa Y.,Ibaraki University | Ichinoseki S.,Itoham Foods Inc. | Tanabe M.,Itoham Foods Inc. | And 2 more authors.
Food Science and Technology Research | Year: 2015

In this study, the effect of glyceraldehyde 3-phosphate dehydrogenase (G3PD) on the molecular state of porcine myofibrils was investigated by observing the structural changes in myosin and actin in myofibrils using phase-contrast and fluorescence microscopy. Though the myofibril gel strength was not influenced by G3PD at a G3PD to myofibril weight ratio (G/M ratio) of 1/20, the gel strength significantly increased at a G/M ratio ≥ 1/10. SDS-PAGE analysis demonstrated that myosin heavy chain band intensity increased in the myofibril soluble fraction by adding G3PD, suggesting G3PD facilitated the solubilization of myosin and actin. Phase-contrast microscopy also showed increased myofibril solubilization with increasing G3PD. Fluorescence microscopy revealed that G3PD colocalized with actin segments. Myosin segments also colocalized with actin segments in G3PD-treated myofibrils, suggesting myosin bound to actin. The addition of G3PD to myofibrils increased the Mg2+- and Mg2+-EGTA-ATPase activities, suggesting G3PD would not change the conformation of myofibrils. Copyright © 2015, Japanese Society for Food Science and Technology.


Sisaphaithong T.,Nagoya University | Kondo D.,Nagoya University | Kondo D.,Itoham Foods Inc. | Matsunaga H.,Nagoya University | And 3 more authors.
Bioscience, Biotechnology and Biochemistry | Year: 2012

Sorghum shows strong growth stimulation on arbuscular mycorrhizal (AM) symbiosis, while barley and wheat show growth depression. We identified the AMinducible phosphate transporter genes of these cereals. Their protein products play major roles in phosphate absorption from arbuscules, intracellular fungal structures. Unexpectedly, barley and wheat expressed the AM-inducible genes at high levels. Hence the cause of their growth depression appears to be unrelated to the transcription of these genes. Notably, fungal vesicles were formed significantly more in barley and wheat than in sorghum. This study yielded new clues for investigation of the mechanism underlying these various responses.


Trademark
Itoham Foods Inc. | Date: 2015-02-16

Beef; meat; processed meat products; processed beef products; pre-cooked curry stew; pre-cooked stew; pre-cooked soup mixes; prepared meals consisting primarily of meat, beef, processed meat products or processed beef products; all meat products from WAGYU cattle.


Trademark
Itoham Foods Inc. | Date: 2016-01-06

Meat; meat offal; processed meat products; prepared meals consisting principally of meat; prepared meals consisting principally of processed meat products; pre-cooked curry stew, stew and soup mixes; processed vegetables and fruits; milk products.


PubMed | Itoham Foods Inc.
Type: Comparative Study | Journal: Animal science journal = Nihon chikusan Gakkaiho | Year: 2013

The purpose of this study was to assess an evaluation method using an artificial taste sensor, in comparison with chemical analysis and sensory evaluation of the taste of meat during curing. Samples of Canadian pork were treated with salt, nitrite and phosphate. Curing time ranged from 0 to 168 h. In the sensory evaluation, there were no significant differences in the all characteristic items at 72-h cured sample compared to the 0-h sample. Some of the characteristic items for the 168-h sample (umami, overall taste, richness and overall palatability) showed significant difference (P < 0.05) compared to the 0-h sample. Taste sensor analysis indicated that the sensor outputs of bitterness and saltiness were significantly correlated with curing time (R = 0.98 and 0.97, respectively), and total free amino acids (R = 0.91 and 0.96, respectively). The sensor output of bitterness was significantly correlated (R = 0.96) with the sum of amino acids corresponding to bitter taste. The increase in the chemical components contributing to bitterness and/or saltiness was indicated as the cause of the characteristic taste. Taste sensor analysis may be applicable as a qualitative method for evaluating taste characteristics generated during the curing of manufactured cooked meat products.

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