Influence of death struggle on the structural changes in chub mackerel muscle during chilled storage

ABSTRACT: Chub mackerel (34–35 cm, approximately 500 g), which were caught by fishing with a rod and line at the Bungo Channel, Oita prefecture, were rested overnight in a fish preserve and either killed by decapitation (control group) or allowed to struggle in air for 30 min (struggled group). Muscle samples were excised every 4 h, and measurements on breaking strength and histological observations were done for both groups. The breaking strength of muscle in the control group was significantly higher than that in the struggled group, whereby a decrease in breaking strength was delayed for 12 h compared to the struggled group. Light microscopy showed space extension among muscle cells in association with a decrease in breaking strength. Especially in the struggled group, the extended area was larger and the difference in area was significant at the time when breaking strength showed a significant difference. Using electron microscopy, the extended area showed cut and/or disappeared collagen fibrils. From these results, it was demonstrated that struggling to death promoted the degradation of collagen fibrils and the weakening of connective tissue and, resultantly, led to the faster softening of muscle of chub mackerel.     

Effect of dipeptide on intestinal peptide transporter 1 gene expression: An evaluation using primary cultured chicken intestinal epithelial cells

Peptide transporter 1 (PepT1) is a transporter responsible for absorbing dipeptide and tripeptide in enterocytes and is upregulated by dipeptide in mammals. It has not been certain whether intestinal PepT1 expression is responsive to dipeptides in chickens because of the lack of in vitro study using the cultured enterocytes. This study established a primary culture model of chicken intestinal epithelial cells (IECs) in two-dimensional monolayer culture using collagen gel by which the response of chicken PepT1 gene expression to dipeptide stimuli was evaluated. The cultured chicken IECs showed the epithelial-like morphology attached in a patch-manner and exhibited positive expression of cytokeratin and epithelial cadherin, specific marker proteins of epithelial cells. Moreover, the chicken IECs exhibited the gene expression of intestinal cell type-specific marker, villin1, mucin 2, and chromogranin A, suggesting that the cultured IECs were composed of enterocytes as well as goblet and enteroendocrine cells. PepT1 gene expression was significantly upregulated by synthetic dipeptide, glycyl-l-glutamine, in the cultured IECs. From the results, we herein suggested that dipeptide is a factor upregulating PepT1 gene expression in chicken IECs.     

The influence of crossbreeding on collagen solubility and tenderness of Infraspinatus and Semimembranosus muscles of semi‐intensively reared young bulls

The aim of the present study was to investigate the effects of crossbreeding on collagen content and solubility, shear force (WBSF) and the eating quality of Infraspinatus (INF) and Semimembranosus (SM) muscles of young bulls and the relationships between collagen content and solubility, shear force and the eating quality of beef. The experimental material comprised muscles of crossbred young bulls (about 600 days old) of Polish Holstein‐Friesian (PHF) × Limousine (LM) (n = 10), PHF × Charolaise (CH) (n = 9), PHF × Hereford (HER) (n = 9) breeds. The crossbreeding influenced WBSF, aroma and taste, total, water‐soluble, acid‐soluble, total soluble and insoluble collagen content, as well as the acid‐soluble, total soluble and insoluble collagen proportions. WBSF was significantly negatively correlated with sensorial tenderness and water‐soluble collagen content. The eating quality of beef obtained from different crossbreds was similar; however, the meat from PHF × LM and PHF × HER bulls had lower WBSF values than PHF × CH bulls. © 2016 Japanese Society of Animal Science     

A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988^T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen.     

Marine Collagen: A Promising Biomaterial for Wound Healing,Skin Anti-Aging,and Bone Regeneration

Marine organisms harbor numerous bioactive substances that can be utilized in the pharmaceutical and cosmetic industries. Scientific research on various applications of collagen extracted from these organisms has become increasingly prevalent. Marine collagen can be used as a biomaterial because it is water soluble, metabolically compatible, and highly accessible. Upon review of the literature, it is evident that marine collagen is a versatile compound capable of healing skin injuries of varying severity, as well as delaying the natural human aging process. From in vitro to in vivo experiments, collagen has demonstrated its ability to invoke keratinocyte and fibroblast migration as well as vascularization of the skin. Additionally, marine collagen and derivatives have proven beneficial and useful for both osteoporosis and osteoarthritis prevention and treatment. Other bone-related diseases may also be targeted by collagen, as it is capable of increasing bone mineral density, mineral deposition, and importantly, osteoblast maturation and proliferation. In this review, we demonstrate the advantages of marine collagen over land animal sources and the biomedical applications of marine collagen related to bone and skin damage. Finally, some limitations of marine collagen are briefly discussed.     

不同养殖模式对中华鳖营养品质的影响

[目的]研究不同养殖模式对中华鳖（Trionyz sinensis）营养品质的影响,为深入探讨提高原生态养殖鳖营养、保健功能的途径和方法提供理论依据.[方法]对原生态、池塘和温室养殖模式下中华鳖肌肉和裙边的基本营养成分及肌肉氨基酸、脂肪酸组成的差异进行比较分析.[结果]与池塘养殖鳖和温室养殖鳖相比,原生态养殖鳖的肌肉蛋白质、脂肪和胶原蛋白含量最高,水分含量最低;裙边水分、蛋白和胶原蛋白含量显著高于池塘养殖鳖和温室养殖鳖（P＜0.05,下同）,但脂肪含量最低.从3种鳖的肌肉中能检测出16种氨基酸,且肌肉氨基酸总量、必需氨基酸和鲜味氨基酸总量均以原生态养殖鳖最高.从中华鳖肌肉中共检测到21种脂肪酸,包括7种饱和脂肪酸、6种单不饱和脂肪酸、8种多不饱和脂肪酸;原生态养殖鳖的单不饱和脂肪酸总量显著高于池塘养殖鳖和温室养殖鳖,温室养殖鳖的不饱和脂肪酸总量最高,但除C18∶2n-6外,其他多不饱和脂肪酸含量均以原生态养殖鳖最高.[结论]原生态养殖鳖的品质优于池塘养殖鳖和温室养殖鳖.     

海燕体壁胶原蛋白提取工艺的初步研究

采用两种不同的方法从海燕Asterina pectinifera体壁中提取出酸溶性胶原蛋白（ASC）和胃蛋白酶促溶性胶原蛋白（PSC）。结果表明：ASC的最佳反应条件是,温度为10℃,提取液种类为乙酸-乙酸钠溶液,提取液浓度为0.5 mol/L,提取时间为72 h,ASC得率为7.93%;PSC的最佳反应条件是,温度为17℃、胃蛋白酶酶加量为4%、提取时间为96 h,PSC得率为49.61%。经紫外光谱和氨基酸组成分析,结果表明,ASC和PSC均为典型的Ⅰ型胶原蛋白。     

A chronic oral toxicity study of marine collagen peptides preparation from chum salmon (Oncorhynchus keta) skin using Sprague-Dawley rat

Due to the increased consumption of marine collagen peptides preparation (MCP) as ingredients in functional foods and pharmaceuticals, it was necessary to carry out safety requirements in the form of an oral chronic toxicity assessment. In order to define the oral chronic toxicity of MCP, a 24-month feeding study of MCP was carried out. Sprague-Dawley (S-D) rats at the age of four-week of both sexes were treated with MCP at the diet concentrations of 0%, 2.25%, 4.5%, 9% and 18% (wt/wt). The actual food intake and bodyweight of the individual animals were recorded periodically until sacrifice. Blood and urine samples were collected for serum chemistry evaluations and urinalysis. Throughout the experimental period, there was no toxicologically significant difference between the vehicle and MCP-treated animals with respect to the survival rate, body weight, food consumption, urinalysis, clinical biochemistry parameter and relative organ weight in either sex. Moreover, incidences of non-neoplastic lesions in MCP-treated groups did not significantly increase compared with the control group. Under the present experimental conditions, no higher risk of chronic toxic effects was observed in MCP-treated rats at the diet concentrations of 2.25%, 4.5%, 9% and 18% (wt/wt) than in the rats fed with basal rodent diet.     

日本鳗鲡胶原蛋白和小清蛋白的过敏原性

以日本鳗鲡皮与肌肉组织为研究对象,采用碱溶、酸溶、盐析、冻干等方法纯化得到胶原蛋白,采用加热、饱和硫酸铵分级盐析、DEAE-Sepharose阴离子交换层析等方法纯化得到两种亚型的小清蛋白(PV-Ⅰ和PV-Ⅱ),纯化的目标蛋白经动物特异性抗体的免疫印迹实验确证。酶联免疫吸附测定和免疫印迹分析结果显示,纯化的胶原蛋白和小清蛋白分别与鱼类过敏患者阳性血清发生特异性反应,且二者之间无免疫交叉反应。体外模拟胃液消化实验和SDS-PAGE分析结果显示,胶原蛋白和小清蛋白均具有较高的消化稳定性。结果提示,日本鳗胶原蛋白和小清蛋白具有较高的消化稳定性和免疫原性,二者可引发不同患者的IgE介导特异性超敏反应。