Collagen Sources and Areas of Use

Cherim, Melat; Mustafa, Alef; Cadâr, Emin; Lupaşcu, Naliana; Paris, Spartaco; Sîrbu, Rodica

doi:10.26417/ejis.v4i1.p122-128

Cited by 7 publications

(5 citation statements)

References 11 publications

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Section: Characteristics Of Collagenmentioning

confidence: 99%

“…In dry skin, a decrease in metabolism is observed. Research suggests that collagen molecules also play a role in the process of cell proliferation, thanks to their ability to bind cytokines, and the stimulation of cell division in the skin is extremely important, especially in the process of regeneration of skin defects [ 30 , 37 , 48 ]. According to research, amino acids derived from the breakdown of fish collagen (glycine and hydroxyproline) [ 3 , 19 ], which was applied to the skin, have a possible impact on the amount of cytokines produced by fibroblasts and keratinocytes.…”

Section: The Importance Of Collagen In the Skinmentioning

confidence: 99%

“…It was observed that hydrolysate applied topically to the skin protected natural collagen against degradation and also had a protective effect on elastin [ 61 ]. Ineffectiveness of topical CLG skin care products may occur due to the inability to penetrate the stratum corneum, which prevents the product from reaching the fibroblasts in the dermis [ 1 , 35 , 40 , 48 ]. Therefore, when it comes to collagen products, the chosen route and how they will be used is important [ 4 , 34 , 39 , 47 , 56 , 57 , 63 , 73 , 79 ].…”

Section: Characteristics Of Cosmetic Products Containing Collagenmentioning

confidence: 99%

“…The most noticeable symptom is the loss of skin firmness and general deterioration of its condition. Hair becomes brittle and falls out excessively, which may lead to premature baldness [17,37,47,48]. Then, the level of estrogens decreases, which affects the synthesis of this protein and changes its properties.…”

Section: Effects Of Collagen Deficiency In the Bodymentioning

confidence: 99%

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Use of Collagen in Cosmetic Products

Jadach,

Mielcarek,

Osmałek

2024

CIMB

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Collagen (CLG) belongs to the family of fibrillar proteins and is composed of left-handed α polypeptide chains, which, twisting around themselves and their axis, form a right-handed superhelix. In the chemical structure, it contains mainly proline, hydroxyproline, glycine, and hydroxylysine. It occurs naturally in the dermis in the form of fibers that provide the skin with proper density and elasticity. The review aimed to present the types of collagen protein, factors affecting its structure and its unusual role in the functioning of the human body. Also, an overview of cosmetic products containing collagen or its derivatives, the characteristics of the formulas of these products, and the effects of their use were presented. Throughout the market, there are many cosmetic and cosmeceutical products containing CLG. They are in the form of fillers administered as injections, belonging to the group of the oldest tissue fillers; products administered orally and for topical use, such as creams, gels, serums, or cosmetic masks. Analyzed studies have shown that the use of products with collagen or its peptides improves the general condition of the skin and delays the aging process by reducing the depth of wrinkles, improving hydration (in the case of oral preparations), reducing transepithelial water loss (TEWL), as well as improving skin density and elasticity. In addition, oral application of bioactive CLG peptides has shown a positive effect on the nails, reducing the frequency of their breakage.

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Section: Characteristics Of Collagenmentioning

confidence: 99%

Section: The Importance Of Collagen In the Skinmentioning

confidence: 99%

Section: Characteristics Of Cosmetic Products Containing Collagenmentioning

confidence: 99%

Section: Effects Of Collagen Deficiency In the Bodymentioning

confidence: 99%

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Use of Collagen in Cosmetic Products

Jadach,

Mielcarek,

Osmałek

2024

CIMB

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“…Perbedaan kandungan hidroksiprolina dapat Amino acid (mg/g) Pink ear emperor fish Tuna (Kaewdang et al, 2014) Red snapper (Jamilah et al, 2013) Ariid catfish (Utami, 2021) Pangas catfish (Sitepu et al, Table 5 Amino acid profile of fish collagen from swim bladders from pink ear emperor fish Tabel 5 Profil asam amino kolagen dari gelembung renang ikan lencam dipengaruhi oleh spesies, lingkungan, dan suhu tubuh ikan (Lin et al, 2020). Kandungan glisina yang tinggi penting karena glisina adalah asam amino yang menyusun sekuens dasar kolagen Gly-X-Y dalam pembentukan tropokolagen (Cherim et al, 2016). Asam amino penyusun kolagen lainnya ialah prolina dan alanina.…”

Section: Profil Asam Amino Kolagen Gelembung Renang Ikan Lencamunclassified

Ekstraksi dan determinasi karakteristik kolagen gelembung renang ikan lencam (Lethrinus lentjan)

Sakinah,

Trilaksani,

Nurhayati

2023

JPHPI

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Ekspor filet ikan lencam yang terus meningkat di Indonesia menyebabkan peningkatan pada jumlah hasil samping produksi, salah satunya gelembung renang. Gelembung renang ikan merupakan sumber alternatif kolagen yang telah menarik minat ilmuwan dan industri untuk diaplikasikan di berbagai sektor kesehatan, farmasi, dan kosmetik. Penelitian ini bertujuan untuk menentukan rasio bahan dan pelarut serta waktu yang optimal pada tahap praperlakuan dalam ekstraksi kolagen dari gelembung renang ikan lencam. Penelitian dibagi menjadi tiga tahapan, yaitu optimasi praperlakuan sampel menggunakan larutan NaOH dengan lama waktu yang berbeda, ekstraksi dengan rasio bahan dan pelarut asam asetat dan penambahan enzim papain, dan karakterisasi kolagen gelembung renang ikan lencam. Analisis komponen gelembung renang ikan lencam meliputi proksimat, asam amino, dan protein terlarut. Analisis kualitas kolagen meliputi proksimat, asam amino, pengukuran warna, derajat putih, pH, pita protein, dan gugus fungsi. Kondisi praperlakuan terbaik didapat pada gelembung renang ikan lencam yang direndam NaOH 0,1 M selama 8 jam. Ekstrasi kolagen gelembung renang ikan lencam terbaik, yaitu rasio 1:30 (b/v) larut enzim papain (PaSC) sebesar 28,88±0,71% selama 48 jam. Kandungan protein mencapai 92,56±0,12%, derajat putih 97,86%, nilai pH 6,64, kandungan hidroksiprolina sebesar 79,32 mg/g, glisina 293,35 mg/g, dan prolina 102,57 mg/g sebagai asam amino penciri kolagen. Hasil deteksi gugus fungsi menunjukkan adanya gugus fungsi amida I, II, III, A, dan B serta rantai α1 dan α2 . Pola protein kolagen terdeteksi pada kisaran molekul 100-250 kDa yang mengindikasikan kolagen tipe I.

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