scholarly journals MOLECULAR STRUCTURE OF GELATIN EXTRACTED FROM PARROT (Scarus sp) FISH SCALES

2020 ◽  
Vol 8 (1) ◽  
pp. 15
Author(s):  
Jeszy Novianti Andakke ◽  
Inneke F M Rumengan ◽  
Hizkia H Y Nainggolan ◽  
Lasma R M E Parapat ◽  
Engel Pandey ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Fourier Transform ◽  
Moisture Content ◽  
Key Words ◽  
Triple Helix ◽  
Fourier Transform Infrared ◽  
Water Soluble ◽  
Wave Number ◽  
Fish Scales ◽  
Single Helix

One of the protein molecules of fish scales is water soluble gelatin. Gelatin of fish scales could be best substitute of commercial available gelatin which derived from porcine and bovine. The purpose of this study was to determine the molecular structure of gelatin extracted from marine fish scale using Fourier transform infrared (FTIR) analysis, and to obtain the moisture content, pH and yield of gelatin. Samples were prepared from the wet and dried scales. As for the standard gelatin, the gelatin of the two samples are characterized with several types of amide groups. The two gelatin samples were slight different in absorption of wave length for amide A, B, I, II and III groups indicating the instability of the functional groups which may influence viscosity and gel strength. For the wet scales derived gelatin, the wave number absorption was found to be 3412 cm-1 (amide A), 2421 cm-1 (amide B), 1653 cm-1 (amide I), 1400 cm-1 (amide II), and 1001 cm-1 (amide III), while for the dried scales derived gelatin was 3435 cm-1 (amide A), 2920 cm-1 (amide B), 1635 cm-1 (amide I), 1404 cm-1 (amide II), and 1036 cm-1 (amide III). The wave number absorption of amide III of gelatin is smaller than the one of collagen, because gelatin is in form of single helix, not triple helix. The wet scales derived and dried scales derived gelatin show the moisture content of 15.0% and 13.7%, and yield of 2.33% and 2.43%, .respectively. For both samples, the pH value was 7. Key words : gelatin, fish scales, molecule structure, moisture, yield, pH Abstrak Salah satu dari molekul protein sisik ikan adalah gelatin larut air. Gelatin sisik ikan dapat menjadi pengganti terbaik dari gelatin komersial yang tersedia yang berasal dari babi dan sapi. Tujuan dari penelitian ini adalah untuk menentukan struktur molekul gelatin yang diekstrak dari sisik ikan laut menggunakan Analisis FTIR (Fourier Transform Infrared), dan untuk mendapatkan kadar air, pH dan rendemen gelatin. Sampel disiapkan dari sisik basah dan sisik kering. Adapun standar gelatin, gelatin dari kedua sampel ditandai dengan beberapa jenis gugus amida. Kedua sampel gelatin sedikit berbeda dalam penyerapan panjang gelombang untuk amida A, B, I, II dan III yang menunjukkan ketidakstabilan kelompok fungsional yang dapat mempengaruhi viskositas dan kekuatan gel. Untuk gelatin sisik basah, panjang gelombang serapan ditemukan pada 3412 cm-1 (amida A), 2421 cm-1 (amida B), 1653 cm-1 (amida I), 1400 cm-1 (amida II), and 1001 cm-1 (amida III), sedangkan untuk gelatin sisik kering adalah 3435 cm-1 (amida A), 2920 cm-1 (amida B), 1635 cm-1 (amida I), 1404 cm-1 (amida II), and 1036 cm-1 (amida III). Panjang gelombang serapan amida III pada gelatin lebih kecil dibanding kolagen, sehingga gelatin berbentuk single helix, bukan triple helix. Gelatin sisik basah dan sisik kering mengadung kadar air 15,0% dan 13,7%, rendemen 2,33% and 2,43%, secara berturut-turut. Untuk kedua sampel memiliki nilai pH 7. Key words : gelatin, sisik ikan, struktur molekul, kadar air, rendemen, pH

scholarly journals PENENTUAN STRUKTUR MOLEKUL KOLAGEN SISIK IKAN KAKATUA (Scarus sp) BERDASARKAN SERAPAN MOLEKUL TERHADAP GELOMBANG FTIR (FOURIER-TRANSFORM INFRARED SPECTROSCOPY ANALYSIS)

2020 ◽  
Vol 8 (1) ◽  
pp. 7
Author(s):  
Shellyn Prastisia Mberato ◽  
Inneke F M Rumengan ◽  
Veibe Warouw ◽  
Stenly Wullur ◽  
Natalie D T Rumampuk ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Functional Groups ◽  
Triple Helix ◽  
Fourier Transform Infrared ◽  
Infrared Region ◽  
Collagen Molecule ◽  
Fish Scale ◽  
Fish Scales ◽  
Pre Treatment ◽  
Parrot Fish

 Parrot fish (Scarus sp) is a commodity which commonly consumed in North Sulawesi. High consumption of this fish has caused the high amount of fish scales as wastes. As parrot fish scales contain protein that could be transformed into commercial products such as collagen. Collagen could be applied in the industrial fields including cosmetics and pharmaceutics.  The purpose of this study was to determine molecular structure of collagen derived from the wet and dry parrot fish (Scarus sp) scales, based on molecular absorption of electromagnetic in the infrared region of the fourier transform infrared spectroscopy.Preparation of collagen of fish scales both in wet and dry forms, was initially performed with pre-treatment of raw materials by maceration in sodium hydroxide (NaOH) solution for 48 hours. Then hydrolysis process was conducted in hydrochloric acid (HCl) solution again for 48 hours to remove mineral contents of the scales.  Collagen yield of fish scales in wet and dry forms was 2.23% and 3.00%, respectively, with pH 7, and the respective  water content was  13% and 12%. For collagen derived from the wet scales, the functional groups of amide A and B absorb the electromagnetic at infrared region of 3429 cm-1 and 2930 cm-1), respectively. Also amide I, II and III absorb the electromagnetic at infrared region of 1657 cm-1, 1452 cm-1 and 1242 cm-1, respectively. It was comparable to that of collagen derived from the dry scales, the functional groups of amide A and B absorb the electromagnetic at infrared region of 3425 cm-1 and 2910 cm-1), respectively. Also amide I, II and III absorb the electromagnetic at infrared region of 1653 cm-1, 1402 cm-1 and 1244 cm-1, respectively.  The amide  III group of  the wet scales derived collagen as well as the dry scales derive collagen absorb the electromagnetics at infrared region in the range of 1309-1229 cm-1 indicating that the fish scale derived collagen has not denatured yet, but still in triple helix structure. Molecular functional groups detected for the parrot fish scales derived collagen are in the range of those for  collagen standard.Keywords : fish scale, Scarus sp, collagen, molecule structure, proximate  AbstrakIkan kakatua (Scarus sp) merupakan salah satu jenis komiditi ikan yang banyak dikonsumsi di Sulawesi Utara. Tingginya konsumsi ikan kakatua berakibat banyaknya limbah kuliner ikan ini berupa sisik ikan. Padahal sisik ikan kakatua mengandung protein yang dapat ditransformasikan menjadi produk samping komersial seperti kolagen. Kolagen dapat diaplikasikan pada bidang industry kosmetik dan farmasika. Tujuan penelitian ini menentukan struktur molekul kolagen dari sisik ikan kakatua (Scarus sp) berdasarkan wilayah serapan gelombang infra red.Preparasi kolagen dari sisik ikan baik dalam bentuk basah maupun kering,  diawali dengan proses pre-treatment bahan baku dengan melakukan perendaman menggunakan larutan NaOH selama 48 jam. Selanjutnya adalah tahap hidrolisis yang dilakukan dengan perendaman sampel menggunakan larutan asam klorida (HCl) selama 48 jam untuk menghilangkan mineral yang ada dalam sisik. Kolagen sisik basah dan sisik kering dari ikan kakatua memiliki nilai rendemen masing-masing sebesar 2.23% dan 3.00%, nilai pH 7 serta kadar air sebesar 13% dan 12%. Pada kolagen sisik basah terdeteksi Amida A mempunyai bilangan gel (3429 cm-1), Amida B (2930 cm-1). Amida I (1657 cm-1), Amida II (1452 cm-1 ) dan Amida III (1242 cm-1), sedangkan pada kolagen sisik kering  terdeteksi Amida A mempunyai bilangan gel (3425 cm -1 ), Amida B (2910 cm-1 ). Amida I (1653 cm-1 ), Amida II (1402 cm-1 ) dan Amida III (1244 cm-1). Amida III pada kolagen sisik basah dan kolagen sisik kering terdeteksi pada wilayah serapan 1309-1229 cm-1 hal menandakan bahwa kolagen sisik  ikan kakatua belum terdenaturasi karena masih terdapat struktur triple helix. Gugus fungsional kolagen sisik kering dan kolagen sisik basah dari ikan kakatua memenuhi standar gugus fungsional kolagen standar.Kata kunci : sisik, Scarus sp, kolagen, gugus fungsi, proksimat

Difference in Molecular Structure of Rod and Cone Visual Pigments Studied by Fourier Transform Infrared Spectroscopy†

Biochemistry ◽  
2001 ◽  
Vol 40 (9) ◽  
pp. 2879-2886 ◽  
Author(s):  
Hiroo Imai ◽  
Takahiro Hirano ◽  
Hideki Kandori ◽  
Akihisa Terakita ◽  
Yoshinori Shichida
Keyword(s):  
Molecular Structure ◽  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Fourier Transform Infrared Spectroscopy ◽  
Fourier Transform Infrared ◽  
Visual Pigments

scholarly journals Assessment of phytochemical screening by Fourier Transform Infrared spectroscopic analysis of peach (Prunus persica) seed biomass from Uttarakhand region of India

2020 ◽  
Vol 12 (4) ◽  
pp. 519-524
Author(s):  
Rishi Kumar Shukla ◽  
Ravi Kant
Keyword(s):  
Fourier Transform ◽  
Ethyl Acetate ◽  
Petroleum Ether ◽  
Prunus Persica ◽  
Fourier Transform Infrared ◽  
Water Soluble ◽  
Physical Parameters ◽  
Crude Fibre ◽  
Soxhlet Apparatus ◽  
Seed Biomass

Prunus persica (Peach) has several medicinal and nutritive properties such as antioxidant, antimalarial, anticoagulant, antifungal, ant-allergic, etc. The present study focuses on the exploratory for phytochemicals constituents screening of seed extracts of  Prunus persica from Uttarakhand region of India by Fourier Transform Infrared spectroscopy (FTIR) analysis. The extraction of seed was carried out using soxhlet apparatus in different solvents such as petroleum ether, chloroform, ethyl acetate, ethanol, and water. The characteristics of physical parameters of dried seed of P. persica were reported  as total ash (14.250±0.126 %), acid insoluble ash (6.800±0.036 %), water-soluble ash (11.714±0.123 %), and sulphated ash value (2.274±0.025 %); whereas, the extractive values were also recorded as alcohol soluble extractive (1.917±0.011 %), and water-soluble extractive (10.580±0.048 %). The highest values of  nutritive components (366.778±0.257 %) were followed by, carbohydrate (45.500±0.336 %), crude protein (29.360±0.551 %), available carbohydrate content (28.002±0.439 %), moisture content (12.547±0.022 %), crude fibre (11.602±0.123 %), crude fat (7.482±0.068 %), and total nitrogen (4.695±0.032 %). The maximum extraction yield was recorded in the aqueous extract solution (11.15 %), followed by petroleum ether (2.8 %), ethyl acetate (2.1 %), ethanol (1.6 %), and chloroform (0.4 %). Besides, this the most effective chemical bonding groups of FTIR spectra analyzed in a sample of P. persica seed were N-H, O-H (3600-3400 1/cm), C-H (3000-2800 1/cm), N-H, C-C, C=O (1680-1550 1/cm), C-H (1470-1350 1/cm), CO-OR (1400-1000 1/cm), C-H (850-550 1/cm), and C-I (500-400 1/cm), respectively. Therefore, this study provides useful insights into the beneficial properties of P. persica seed biomass from the Uttarakhand region of India, which may be further used for the production of several pharmaceuticals and nutraceutical products.

scholarly journals Isolation of papain-soluble collagen from the skin of snake-head fish (Channa striata)

2020 ◽  
pp. 87-93
Author(s):  
Andi Rahmayanti Ramli ◽  
Andi Rezky Annisa ◽  
Nur Alim Bahmid ◽  
Muhammad Dalvi Mustafa
Keyword(s):  
Fourier Transform ◽  
Moisture Content ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fourier Transform Infrared ◽  
Helical Structure ◽  
Collagen Type I ◽  
Type I ◽  
Fish Skin ◽  
Soluble Collagen ◽  
Channa Striata

Snake-head fish (Channa striata) skin categorized a byproduct contains a higher concentration of collagen. The collagen can be extracted by using protease, which is known as Papain Soluble Collagen (PaSC). This study aimed to isolate the collagen from the snake-head fish skin using papain. The yield percentage and moisture content of PaSC in the skin was determined. Measurements using SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) were performed to characterize the PaSC and its functional groups. The results showed that the yields and moisture content of PaSC were 8.9% and 6.07%, respectively. The PaSC characterized by two α-chains appeared as collagen type I. Fourier transform infrared (FTIR) spectra of PaSC confirmed a triple-helical structure of collagen. The results indicated that snake-head fish skin could be used as potential resources of collagen and papain can be used as an alternative affordable enzyme.

Fourier Transform Infrared Spectroscopy Evidence of the Nanoscale Structural Jump in Medium-Rank Tectonic Coal

2021 ◽  
Vol 21 (1) ◽  
pp. 636-645
Author(s):  
Xiaobing Zhang ◽  
Tianrang Jia ◽  
Hang Zhang ◽  
Yiwen Ju ◽  
Yugui Zhang
Keyword(s):  
Molecular Structure ◽  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Fourier Transform Infrared Spectroscopy ◽  
Structural Parameters ◽  
Fourier Transform Infrared ◽  
Structure Evolution ◽  
Side Chains ◽  
Aromatic System ◽  
Tectonic Coal

Coal is a pressure-sensitive organic rock. The effect of tectonism on the structural evolution of medium-rank coal has been confirmed by the change in the crystal state of tectonic coal, but the organic molecular level response has not been reported. In this paper, three sets of medium-rank tectonic coals and symbiotic nontectonic coals were selected. The distributions of their functional groups and their molecular structure evolution were assessed using Fourier Transform Infrared Spectroscopy (FTIR), and their structural parameters were determined from the curve-fitting analysis. The nanoscale structural jump characteristics and mechanisms of medium-rank tectonic coal were revealed. Compared with symbiotic nontectonic coal, tectonism accelerated the exfoliation of side chains (groups) in the macromolecular structure, enlarged the aromatic system, and removed the unstable groups such as associative hydrogen bonds at first, which indicated that the molecular structure of tectonic coal was affected by nanoscale deformation, showing obvious advanced evolution characteristics. For the fat coal, the removal of side chains (groups) during the formation of tectonic coal makes the aromatic ring condensation obvious. For the coking coal, the formation of tectonic coal is dominated by cycloaliphatic dehydrogenation and aromatization, accompanied by the condensation of the aromatic rings. The tectonic coal formed from lean coal shows obvious aromatization characteristics. The molecular depolymerization and chemical tailoring caused by tectonism promotes the removal of hydrophobic side chains (groups) and activates some polar structure sites in coal. It is considered that the nanoscale structural jump of medium-rank tectonic coal is the result of the competition between the aromatic system and aliphatic structures.

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