(−)-Epigallocatechin gallate protected molecular structure of collagen fibers in sea cucumber Apostichopus japonicus body wall during thermal treatment

Dong, Xiufang; Shen, Ping; Yu, Meiqi; Yu, Chenxu; Zhu, Beiwei; Qi, Honglan

doi:10.1016/j.lwt.2020.109076

Cited by 23 publications

(21 citation statements)

References 23 publications

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“…Thus, current research interest is directed towards the use of marine invertebrates as potential sources of collagen, particularly for biomedical applications. Recent investigations have been concentrated on jellyfish [ 92 ] sponges [ 93 ], mussels [ 4 , 94 ], and sea cucumber [ 14 , 16 , 83 , 95 , 96 , 97 , 98 , 99 , 100 , 101 , 102 , 103 , 104 , 105 ] as potential candidates for producing marine-derived collagen.…”

Section: Sources Of Collagenmentioning

confidence: 99%

“…Furthermore, previous studies have reported the effect of thermal treatment on collagen fibrils in relation to oxidation [ 139 ]. A recent study investigated the molecular structure of collagen isolated from Apostichopus japonicus during thermal treatment in the presence of (-)-epigallocatechin gallate (EGCG) [ 105 ] and demonstrated that EGCG has the potential to enhance the thermal stability of crude collagen fibrils by neutralizing the effect of heat-induced radicals (hydroxyl radical) and protect the macromolecular structure of crude collagen in a dose-dependent manner [ 105 ].…”

Section: Characteristics and Properties Of Collagen Type Imentioning

confidence: 99%

“…The RP-HPLC method is often employed for the separation of low-molecular-weight peptides and for amino acid analysis. Dong et al [ 105 ] investigated the molecular weight distribution of collagen peptides isolated from Apostichopus japonicus . Zhu et al [ 95 ] further purified the pepsin soluble collagen isolated from Stichopus japonicus by removing carbohydrate moieties from the collagen fibrils and used a multi-step gradient elution system coupled with a UV-visible spectroscopy to detect the collagen and carbohydrate peaks separately.…”

Section: Pre-treatment Extraction Isolation and Purificationmentioning

confidence: 99%

“…Fourier transform infrared (FTIR) spectroscopy is another popular technique for analyzing the structure of proteins, especially characterization of their secondary structure. In collagen characterization studies, FTIR spectroscopy plays a vital role as it allows confirmation by absorption wavenumber of each amide band [ 105 ].…”

Section: Pre-treatment Extraction Isolation and Purificationmentioning

confidence: 99%

“…Among the amide bands, amide I band is considered as being a crucial factor in determining the secondary structure of protein molecules. Analysis of the amide I band in infrared (IR) spectra indicates the characteristic structural changes of triple helix in the collagen molecule that are stabilized by hydrogen bonds present in C=O and adjacent groups [ 105 ]. Furthermore, the triple helical structure of collagen is confirmed from the absorption ratio between 1236.5 and 1449.5 cm −1 of amide III band, which is approximately equal to 1.0 [ 95 , 99 ].…”

Section: Pre-treatment Extraction Isolation and Purificationmentioning

confidence: 99%

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Sea Cucumber Derived Type I Collagen: A Comprehensive Review

2020

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Collagen is the major fibrillar protein in most living organisms. Among the different types of collagen, type I collagen is the most abundant one in tissues of marine invertebrates. Due to the health-related risk factors and religious constraints, use of mammalian derived collagen has been limited. This triggers the search for alternative sources of collagen for both food and non-food applications. In this regard, numerous studies have been conducted on maximizing the utilization of seafood processing by-products and address the need for collagen. However, less attention has been given to marine invertebrates and their by-products. The present review has focused on identifying sea cucumber as a potential source of collagen and discusses the general scope of collagen extraction, isolation, characterization, and physicochemical properties along with opportunities and challenges for utilizing marine-derived collagen.

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