Effects of Glasswort and Pepsin-Soluble Collagen on Processing Characteristics of Low-Salt Pork Patties

2019 ◽  
Vol 35 (02) ◽  
pp. 187-197
Author(s):  
Dong-Heon Song ◽  
Youn-Kyung Ham ◽  
Ko-Eun Hwang ◽  
Koo Bok Chin ◽  
Hyun-Wook Kim
2017 ◽  
Vol 26 (5) ◽  
pp. 502-515 ◽  
Author(s):  
Saijun Lin ◽  
Ya-Ping Xue ◽  
Enli San ◽  
Tan Chee Keong ◽  
Lifang Chen ◽  
...  

2019 ◽  
Vol 23 (5) ◽  
pp. 183-195
Author(s):  
Settakorn Upasen ◽  
Kornrat Naeramitmarnsuk ◽  
Christian Antonio ◽  
Susan Roces ◽  
Héctor Morillas ◽  
...  

2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu

Pepsin-soluble collagen (PSC) was successfully extracted from the skin of Amiurus nebulosus. The skin of Amiurus nebulosus was immersed in 0.3 mol/L acetic acid (1: 20, m: V) for 6 h at 37°C, while pepsin was added, at a level of 5000U/g dosage of defatted skin. The maximal yield of the collagen was 97.44%, which was higher than that of acid-soluble collagen (ASC) at 62.05%. Some properties of pepsin-soluble collagens from the skin of Amiurus nebulosus were characterized. Amino acid composition and SDS-PAGE suggested that the collagen might be classified as type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements in PSC of Amiurus nebulosus skin of collagen. There is a possibility to use Amiurus nebulosus skin collagen as an alternative source of collagen for industrial purposes and subsequently it may maximize the economical value of the fish.


2021 ◽  
Vol 24 (12) ◽  
pp. 406-414
Author(s):  
Rachanimuk Hiransuchalert ◽  
Nakaweerada Oonwiset ◽  
Yolrawee Imarom ◽  
Parinya Chindudsadeegul ◽  
Penchan Laongmanee ◽  
...  

Food Research ◽  
2020 ◽  
Vol 4 (6) ◽  
pp. 2272-2280
Author(s):  
A.W. Sulaiman ◽  
N.M. Sarbon

Fish waste management is one of the biggest impacts towards the environment. However, it is one of the rich sources of protein. Therefore, the aim of this study was to isolate and characterize acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from shortfin scad (Decapterus macrosoma) waste, with the yields of ASC (3.35±3.43%) and PSC (0.10±0.13%) respectively. The isolated ASC and PSC from shortfin scad waste were characterized on chemical composition, protein concentration, structural properties by FTIR, solubility and morphology properties compared to the commercial collagen from tilapia (Oreochromis niloticus) scales. In terms of chemical composition, PSC showed better than ASC, since it contains comparatively higher in protein (26.97±1.02%) by Kjeldahl method and protein concentration (2.69±0.47 mg/mL) by biuret method, compared to ASC. The FTIR investigations also certified the existence of spacial triplehelical structures of collagens that are important for collagen backbones. Solubility results showed that both ASC and PSC are high insolubility at acidic pH with the lowest solubilisation point at the range of alkali condition. The morphological analysis of both ASC and PSC were almost similar too, as there were fibrils and porous structure. Therefore, collagen from shortfin scad waste, could be a useful alternative, with the potential to be used in food ingredient, biomedical, pharmaceutical and nutraceuticals industries


2018 ◽  
Vol 21 (3) ◽  
pp. 513
Author(s):  
Bagus Fajar Pamungkas ◽  
Supriyadi Supriyadi ◽  
Agnes Murdiati ◽  
Retno Indrati

Characteristics of collagen are influenced by the source of raw materials and extraction methods used. The aim of this research was to characterize the acid- and pepsin-soluble collagens from the dry scales of the striped snakehead (Channa striatus). Collagen was extracted using to methods including 0.5 M acetic acid and 0.1% pepsin. The yield of acid soluble collagen (KLA-SH) and pepsin soluble collagen (KLP-SH) were 0.98% and 1.94%, respectively. KLA-SH and KLP-SH contained glycine as the major amino acid and had high imino acid group content i.e 226 and 230 residues/1.000 residues, respectively. FTIR spectra of KLA-SH and KLP-SH showed that of the structure of collagen could be maintained in the form of triple helix structure. KLA-SH and KLP-SH consisted of α1- and α2-chain, β-chain, and γ-chain and is suggested as type I collagen.


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