Jellice Co.

Miyagi, Japan

Jellice Co.

Miyagi, Japan
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News Article | May 4, 2017
Site: marketersmedia.com

Wiseguyreports.Com Adds “Gelatin -Market Demand, Growth, Opportunities and Analysis of Top Key Player Forecast To 2022” To Its Research Database This report studies Gelatin in Global market, especially in North America, China, Europe, Southeast Asia, Japan and India, with production, revenue, consumption, import and export in these regions, from 2012 to 2016, and forecast to 2022. This report focuses on top manufacturers in global market, with production, price, revenue and market share for each manufacturer, covering By types, the market can be split into By Application, the market can be split into Pharmaceutical Food Other By Regions, this report covers (we can add the regions/countries as you want) North America China Europe Southeast Asia Japan India Global Gelatin Market Professional Survey Report 2017 1 Industry Overview of Gelatin 1.1 Definition and Specifications of Gelatin 1.1.1 Definition of Gelatin 1.1.2 Specifications of Gelatin 1.2 Classification of Gelatin 1.2.1 Skin Gelatin 1.2.2 Bone Gelatin 1.2.3 Halal Gelatin 1.3 Applications of Gelatin 1.3.1 Pharmaceutical 1.3.2 Food 1.3.3 Other 1.4 Market Segment by Regions 1.4.1 North America 1.4.2 China 1.4.3 Europe 1.4.4 Southeast Asia 1.4.5 Japan 1.4.6 India 8 Major Manufacturers Analysis of Gelatin 8.1 Gelita 8.1.1 Company Profile 8.1.2 Product Picture and Specifications 8.1.2.1 Product A 8.1.2.2 Product B 8.1.3 Gelita 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.1.4 Gelita 2016 Gelatin Business Region Distribution Analysis 8.2 Rousselot 8.2.1 Company Profile 8.2.2 Product Picture and Specifications 8.2.2.1 Product A 8.2.2.2 Product B 8.2.3 Rousselot 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.2.4 Rousselot 2016 Gelatin Business Region Distribution Analysis 8.3 PB (Tessenderlo) 8.3.1 Company Profile 8.3.2 Product Picture and Specifications 8.3.2.1 Product A 8.3.2.2 Product B 8.3.3 PB (Tessenderlo) 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.3.4 PB (Tessenderlo) 2016 Gelatin Business Region Distribution Analysis 8.4 Nitta 8.4.1 Company Profile 8.4.2 Product Picture and Specifications 8.4.2.1 Product A 8.4.2.2 Product B 8.4.3 Nitta 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.4.4 Nitta 2016 Gelatin Business Region Distribution Analysis 8.5 Qinghai Gelatin 8.5.1 Company Profile 8.5.2 Product Picture and Specifications 8.5.2.1 Product A 8.5.2.2 Product B 8.5.3 Qinghai Gelatin 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.5.4 Qinghai Gelatin 2016 Gelatin Business Region Distribution Analysis 8.6 Dongbao Bio-Tec 8.6.1 Company Profile 8.6.2 Product Picture and Specifications 8.6.2.1 Product A 8.6.2.2 Product B 8.6.3 Dongbao Bio-Tec 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.6.4 Dongbao Bio-Tec 2016 Gelatin Business Region Distribution Analysis 8.7 Weishardt Group 8.7.1 Company Profile 8.7.2 Product Picture and Specifications 8.7.2.1 Product A 8.7.2.2 Product B 8.7.3 Weishardt Group 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.7.4 Weishardt Group 2016 Gelatin Business Region Distribution Analysis 8.8 Sterling Gelatin 8.8.1 Company Profile 8.8.2 Product Picture and Specifications 8.8.2.1 Product A 8.8.2.2 Product B 8.8.3 Sterling Gelatin 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.8.4 Sterling Gelatin 2016 Gelatin Business Region Distribution Analysis 8.9 Ewald Gelatine 8.9.1 Company Profile 8.9.2 Product Picture and Specifications 8.9.2.1 Product A 8.9.2.2 Product B 8.9.3 Ewald Gelatine 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.9.4 Ewald Gelatine 2016 Gelatin Business Region Distribution Analysis 8.10 Italgelatine 8.10.1 Company Profile 8.10.2 Product Picture and Specifications 8.10.2.1 Product A 8.10.2.2 Product B 8.10.3 Italgelatine 2016 Gelatin Sales, Ex-factory Price, Revenue, Gross Margin Analysis 8.10.4 Italgelatine 2016 Gelatin Business Region Distribution Analysis 8.11 Lapi Gelatine 8.12 Great Lakes Gelatin 8.13 Junca Gelatins 8.14 Trobas Gelatine 8.15 Norland 8.16 El Nasr Gelatin 8.17 Nippi Gelatin Division 8.18 India Gelatine & Chemicals 8.19 Geltech 8.20 Reinert Gruppe Ingredients 8.21 Narmada Gelatines 8.22 Jellice 8.23 Vyse Gelatin 8.24 Sam Mi Industrial 8.25 Geliko 8.26 BBCA Gelatin 8.27 Qunli Gelatin Chemical 8.28 Yasin Gelatin Manufacturer 8.29 Xiamen Hyfine Gelatin 8.30 Cda Gelatin For more information, please visit https://www.wiseguyreports.com/sample-request/1241545-global-gelatin-market-professional-survey-report-2017


Yamamoto S.,Jellice Co. | Deguchi K.,Medical Care Proteomics Biotechnology Co. | Onuma M.,Jellice Co. | Numata N.,Jellice Co. | Sakai Y.,Jellice Co.
Biological and Pharmaceutical Bulletin | Year: 2016

Collagen tripeptide (CTP) is a collagen hydrolysate containing a high concentration of tripeptides with a Gly-X-Y sequence, such as Gly-Pro-Hyp. To test the effects of this preparation, we compared the absorption of peptides in humans after ingestion of a tripeptide fraction of CTP (CTP-100), a CTP preparation containing ca. 50% Gly-X-Y tripeptides (CTP-50), and a collagen peptide that did not contain tripeptides (CP). The postprandial levels of Gly-Pro-Hyp and Pro-Hyp in the plasma increased in those subjects who ingested CTP-100 and CTP-50, and were higher with greater Gly-Pro-Hyp ingestion. This demonstrated that collagen hydrolysates were efficiently absorbed when the collagen was ingested in the tripeptide form. Gly-Pro-Hyp and Pro-Hyp were also found in the urine after ingestion of CTP-100 or CTP-50. Similar to the results for the plasma concentration, the urinary excretion of Gly-Pro-Hyp and Pro-Hyp was also dependent on the amount of Gly-Pro-Hyp ingested. This indicates that ingested Gly-Pro-Hyp and generated Pro-Hyp were relatively stable in the body and were transported to the urine in the peptide form. The concentration of Hyp-Gly in the plasma was low after the ingestion of CP and CTP-100 but higher after the ingestion of CTP-50. Overall, our results suggest that tripeptides derived from collagen are absorbed efficiently by the body. © 2016 The Pharmaceutical Society of Japan.


Kanayama Y.,Jellice Co. | Aoki C.,Jellice Co. | Kawai N.,Wakayama Medical University | Sato M.,Wakayama Medical University | Sakai Y.,Jellice Co.
Biological and Pharmaceutical Bulletin | Year: 2014

The purpose of this study was to clarify the adsorption of cisplatin on regenerative-medicine (RM) gelatin sponge, and to verify the relationship between the cisplatin release pattern of cisplatin-adsorbed RM gelatin sponge and the dissolving time of RM gelatin sponge. We tested various RM gelatin sponges, one with a molecular weight of 50000 Daltons (RM-50 gelatin sponge) that is 100% saline soluble at 24 h, RM-50-120 (heated at 120°C) that is 54.3% saline soluble at 24 h, and RM-50-140 (heated at 140°C) that is 15.8% saline soluble at 24h. We investigated the production of cisplatin-adsorbed RM gelatin sponge and measured free cisplatin released from cisplatin-adsorbed RM gelatin sponge. There was no significant difference in the weight of adsorbed cisplatin among the RM-50, RM-50-120, and RM-50-140. The results mean that cisplatin adsorbs onto RM gelatin sponge irrespective of heating temperature. The average adsorbed weight of cisplatin per gram of RM gelatin sponge was 29.3 mg, which was approximately five times more than that per g previously reported for Gelpart (non-soluble gelatin sponge, clinically available). Cisplatin release in the RM-50 gelatin was the most rapid at only 1 h after incubation; it was released gradually and increasingly in the RM-50-120 gelatin, and released slowly in the RM-50-140 gelatin for 24 h incubation. Cisplatin-adsorbed RM gelatin sponge released cisplatin proportional to the dissolving time of RM gelatin sponge, indicating that the cisplatin release time can be controlled by heating for sterilization of RM gelatin sponge. © 2014 The Pharmaceutical Society of Japan.


Okawa T.,Yokohama City University | Yamaguchi Y.,Yokohama City University | Takada S.,Yokohama City University | Sakai Y.,Jellice Co. | And 5 more authors.
Journal of Dermatological Science | Year: 2012

Background: Dry skin causes pruritus and discomfort in patients with xerosis and atopic dermatitis. General treatment for skin dryness involves the topical application of an emollient. However, more effective, simpler therapies are desired. Collagen tripeptide (CTP) is a highly purified, non-antigenic, low-allergenic collagen fraction that is known to have various biological effects. Objective: To clarify the therapeutic effects of CTP for dry skin using acetone-induced dry skin model mice. Methods: ICR mice were treated with acetone followed by oral administration of CTP (80 or 500. mg/kg/day) for 3 days. Hyaluronic acid production induced by CTP was assessed using human dermal fibroblasts in vitro and in an acetone-induced dry skin model mice in vivo. Transepidermal water loss (TEWL) and scratching behavior were evaluated. Furthermore, the effects of CTP on intraepidermal nerve fibers and expression of semaphorin 3A (Sema3A) and nerve growth factor (NGF) were examined by immunohistochemistry and quantitative RT-PCR. Results: CTP enhanced hyaluronic acid production in human dermal fibroblasts in vitro and in murine skin in vivo. Oral administration of CTP in acetone-induced dry skin model mice significantly decreased TEWL and suppressed scratching behavior. Intraepidermal nerve growth was dramatically inhibited in CTP-treated mice. Quantitative PCR analysis and immunohistochemical study revealed that CTP abolished the increased NGF and decreased Sema3A levels induced by acetone treatment. Conclusion: Oral administration of CTP improves dry skin and normalizes axon-guidance factors in the epidermis in addition to reducing pruritus. CTP may be used in a new therapeutic strategy against dry skin and pruritus. © 2012 Japanese Society for Investigative Dermatology.


Unuma H.,Yamagata University | Matsushima Y.,Yamagata University | Furusawa T.,Yamagata University | Sakai Y.,Jellice Co.
Funtai Oyobi Fummatsu Yakin/Journal of the Japan Society of Powder and Powder Metallurgy | Year: 2016

Combination of two or more materials has been and can be a potential strategy to design and develop new biomaterials. For ages, glass ionomer cement and hydroxyapatite-coated titanium implants have been good examples. This article describes other new polymer-ceramic composite biomaterials which have been evidenced to show better efficacy; poly (ethylene terephthalate) coated with gelatin and low crystallinity hydroxyapatite for guided bone regeneration (PET membrane), calcium phosphate cement (CPC) with controlled setting behavior, and gelatin-coated β-TCP scaffold with enhanced mechanical strength and cytocompatibility. In vivo tests of PET membrane showed that the membrane promoted new bone formation, which was supported by in vitro tests evidencing the proliferation and calcification of osteoblasts on the PET membrane. Control of the setting behavior CPC has long been a challenge. The authors coated tetra calcium phosphate, one of the components of CPC, with gelatin because the setting liquid containing gelatin undergoes reversible sol-gel transition at a temperature between room temperature and body temperature. Gelled gelatin retards the setting reactions to proceed whereas gelatin sol does not hinder the reactions to take place. As the result, the CPC paste showed fluidity for 60 minutes at room temperature while set within 3 minutes at the body temperature. Reinforcement of porous β-TCP scaffolds has also been longed for. The authors coated porous β-TCP with gelatin, and prepared scaffolds with 92 % porosity and compressive strength of 5.1 MPa. The gelatin coating also improved in vivo cytocompatibility.


Hayasaka F.,Jellice Co. | Yamamoto S.,Jellice Co. | Sakai Y.,Jellice Co.
Food Science and Technology Research | Year: 2016

In this study, a new method for producing cyclo(-Gly-Pro) using collagen as a raw material was examined. First, collagen was enzymatically hydrolysed and purified to obtain collagen tripeptide (CTP), rich in "Gly-X-Y" tripeptides. After heating this product under atmospheric pressure in an aqueous solution at 95? for 24 h, purification was achieved by reverse-phase column chromatography. The isolated component was confirmed to be cyclo(-Gly-Pro) through structural analysis by MS and NMR spectroscopies. Purity was determined to be 93.6%, and the recovery rate from CTP was 22%, indicating that much Gly-Pro-Y in CTP contributed to cyclization. The cyclization rate from Gly-Pro-Hyp or Gly-Pro-Ala was much higher than that of Gly-Pro, suggesting that cyclo(-Gly-Pro) was efficiently generated from the Gly-Pro-Y sequence. In summary, this is a simple, practical manufacturing method for producing cyclo(-Gly-Pro) from collagen at low cost with high efficiency. © 2016, Japanese Society for Food Science and Technology.


Disclosed are a novel therapeutic agent and a novel prophylactic agent for atherosclerosis, a blood cholesterol level-lowering agent, and a functional food or a food for specified health uses effective for the inhibition and/or prevention of aging of blood vessels or inflammation in blood vessels. Specifically disclosed are an inhibitor of the progression of atherosclerosis, a prophylactic agent for atherosclerosis, a blood cholesterol level-lowering agent, and a functional food and a food for specified health uses both effective for the inhibition and/or prevention of aging of blood vessels or inflammation in blood vessels, each of which comprises, as an active ingredient, a hydrolysis product of a collagen comprising at least one collagen tripeptide Gly-X-Y [wherein Gly-X-Y represents an amino acid sequence; and X and Y independently represent an amino acid residue other than Gly].


Disclosed are a novel therapeutic agent and a novel prophylactic agent for atherosclerosis, a blood cholesterol level-lowering agent, and a functional food or a food for specified health uses effective for the inhibition and/or prevention of aging of blood vessels or inflammation in blood vessels. Specifically disclosed are an inhibitor of the progression of atherosclerosis, a prophylactic agent for atherosclerosis, a blood cholesterol level-lowering agent, and a functional food and a food for specified health uses both effective for the inhibition and/or prevention of aging of blood vessels or inflammation in blood vessels, each of which comprises, as an active ingredient, a hydrolysis product of a collagen comprising at least one collagen tripeptide Gly-X-Y [wherein Gly-X-Y represents an amino acid sequence; and X and Y independently represent an amino acid residue other than Gly].


PubMed | Jellice Co.
Type: Journal Article | Journal: Biological & pharmaceutical bulletin | Year: 2014

The purpose of this study was to clarify the adsorption of cisplatin on regenerative-medicine (RM) gelatin sponge, and to verify the relationship between the cisplatin release pattern of cisplatin-adsorbed RM gelatin sponge and the dissolving time of RM gelatin sponge. We tested various RM gelatin sponges, one with a molecular weight of 50000 Daltons (RM-50 gelatin sponge) that is 100% saline soluble at 24 h, RM-50-120 (heated at 120C) that is 54.3% saline soluble at 24 h, and RM-50-140 (heated at 140C) that is 15.8% saline soluble at 24 h. We investigated the production of cisplatin-adsorbed RM gelatin sponge and measured free cisplatin released from cisplatin-adsorbed RM gelatin sponge. There was no significant difference in the weight of adsorbed cisplatin among the RM-50, RM-50-120, and RM-50-140. The results mean that cisplatin adsorbs onto RM gelatin sponge irrespective of heating temperature. The average adsorbed weight of cisplatin per gram of RM gelatin sponge was 29.3 mg, which was approximately five times more than that per g previously reported for Gelpart (non-soluble gelatin sponge, clinically available). Cisplatin release in the RM-50 gelatin was the most rapid at only 1 h after incubation; it was released gradually and increasingly in the RM-50-120 gelatin, and released slowly in the RM-50-140 gelatin for 24 h incubation. Cisplatin-adsorbed RM gelatin sponge released cisplatin proportional to the dissolving time of RM gelatin sponge, indicating that the cisplatin release time can be controlled by heating for sterilization of RM gelatin sponge.


PubMed | Jellice Co.
Type: Clinical Trial | Journal: Biological & pharmaceutical bulletin | Year: 2016

Collagen tripeptide (CTP) is a collagen hydrolysate containing a high concentration of tripeptides with a Gly-X-Y sequence, such as Gly-Pro-Hyp. To test the effects of this preparation, we compared the absorption of peptides in humans after ingestion of a tripeptide fraction of CTP (CTP-100), a CTP preparation containing ca. 50% Gly-X-Y tripeptides (CTP-50), and a collagen peptide that did not contain tripeptides (CP). The postprandial levels of Gly-Pro-Hyp and Pro-Hyp in the plasma increased in those subjects who ingested CTP-100 and CTP-50, and were higher with greater Gly-Pro-Hyp ingestion. This demonstrated that collagen hydrolysates were efficiently absorbed when the collagen was ingested in the tripeptide form. Gly-Pro-Hyp and Pro-Hyp were also found in the urine after ingestion of CTP-100 or CTP-50. Similar to the results for the plasma concentration, the urinary excretion of Gly-Pro-Hyp and Pro-Hyp was also dependent on the amount of Gly-Pro-Hyp ingested. This indicates that ingested Gly-Pro-Hyp and generated Pro-Hyp were relatively stable in the body and were transported to the urine in the peptide form. The concentration of Hyp-Gly in the plasma was low after the ingestion of CP and CTP-100 but higher after the ingestion of CTP-50. Overall, our results suggest that tripeptides derived from collagen are absorbed efficiently by the body.

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