Process Optimization and Characterizations of Enzyme-Extracted and Acid-Extracted Collagen from Scale of Bighead Carp

Collagen is an important biomedical material. Enzyme (papain) extracted collagen (EEC) and acid (citric acid) extracted collagen (AEC) were isolated from the scale of bighead carp. The process conditions of EEC and AEC were optimized, by orthogonal test method , to be: liquid/solid ratio 20 mL/g, extraction time 48 min, papain concentration 9.52×10-5 mol/L, temperature 28°C for EEC and liquid/solid ratio 20 mL/g, extraction time 36 min, citric acid concentration 0.5 mol/L, temperature 28°C for AEC.Under the optimal conditions the maximum extraction rates were 31.20% for EEC and 9.22% for AEC, respectively. Both EEC and AEC were characterized basically as type I collagen by UV spectra, infrared spectra and amino acid compositions.

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Optimization of Betalain Pigments Extraction Using Beetroot by-Products as a Valuable Source

Inventions ◽

10.3390/inventions6030050 ◽

2021 ◽

Vol 6 (3) ◽

pp. 50

Author(s):

Silvia Lazăr (Mistrianu) ◽

Oana Emilia Constantin ◽

Nicoleta Stănciuc ◽

Iuliana Aprodu ◽

Constantin Croitoru ◽

...

Keyword(s):

Citric Acid ◽

Acid Concentration ◽

Ethanol Concentration ◽

Extraction Process ◽

Extraction Time ◽

Quadratic Model ◽

Citric Acid Concentration ◽

Operating Variables ◽

Conventional Solvent Extraction ◽

Optimized Conditions

(1) Background: This study is designed to extract the bioactive compounds from beetroot peel for future use in the food industry. (2) Methods: Spectrophotometry techniques analyzed the effect of conventional solvent extraction on betalains and polyphenolic compounds from beetroot peels. Several treatments by varying for factors (ethanol and citric acid concentration, temperature, and time) were applied to the beetroot peel samples. A Central Composite Design (CCD) has been used to investigate the effect of the extraction parameters on the extraction steps and optimize the betalains and total polyphenols extraction from beetroot. A quadratic model was suggested for all the parameters analyzed and used. (3) Results: The maximum and minimum variables investigated in the experimental plan in the coded form are citric acid concentration (0.10–1.5%), ethanol concentration (10–50%), operating temperature (20–60 °C), and extraction time (15–50 min). The experimental design revealed variation in betalain content ranging from 0.29 to 1.44 mg/g DW, and the yield of polyphenolic varied from 1.64 to 2.74 mg/g DW. The optimized conditions for the maximum recovery of betalains and phenols were citric acid concentration 1.5%, ethanol concentration 50%, temperature 52.52 °C, and extraction time 49.9 min. (4) Conclusions: Overall, it can be noted that the extraction process can be improved by adjusting operating variables in order to maximize the model responses.

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Extraction Optimization and Characterization of Collagen from Yellow Pike Conger Swimbladder with Acid-Hydro-Exctraction Method

Jurnal Pengolahan Hasil Perikanan Indonesia ◽

10.17844/jphpi.v19i2.13461 ◽

2016 ◽

Vol 19 (2) ◽

pp. 156 ◽

Cited By ~ 3

Author(s):

Fernandy Djailani ◽

Win Trilaksani ◽

Tati Nurhayati

Keyword(s):

Amino Acid ◽

Acid Content ◽

Type I Collagen ◽

Amino Acid Content ◽

Extraction Time ◽

Yield Response ◽

Type I ◽

Alternative Source ◽

Extraction Optimization ◽

Ft Ir

Swim bladder is one of marine potential byproducts for alternative source of collagen. This study aimed to optimize hydro-extraction and characterized collagen. Extraction optimization of collagen was determined using Box-behnken design response surface method with three variables: CH3COOH concentration, soaking time and extraction time to yield response. Hydro-extraction collagen was characterization based on the amino acid content, SDS-PAGE, FT-IR and DSC. Acording to the result, the concentration had significantly influence yield. Optimum extraction conditions were variable combinations of acetic acid concentration of 0.1 M, for 1 h and hydro-extraction time of 1 h to produce the highest yield 63.35%. collagen was classified as type I collagen by amino acid content, electrophoresis patterns and fourier transform infrared (FTIR) spectra. The glass transition of collagen was 67.23oC, showed high thermal stability that can be applied to the cosmetics industry and nutraceutical.

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PENGARUH KONSENTRASI ASAM ASETAT DAN WAKTU EKSTRAKSI TERHADAP MUTU KOLAGEN KULIT NILA HITAMPENGARUH KONSENTRASI ASAM ASETAT DAN WAKTU EKSTRAKSI TERHADAP MUTU KOLAGEN KULIT NILA HITAM

Jurnal Teknosains ◽

10.22146/teknosains.3987 ◽

2011 ◽

Vol 1 (1) ◽

Author(s):

Latif Sahubawa ◽

A.B. Naro Putra

Keyword(s):

Acetic Acid ◽

Type I Collagen ◽

Value Added ◽

Extraction Time ◽

Quantitative Composition ◽

Type I ◽

Industry Waste ◽

Sds Page ◽

Acid Molarity

The objective of the research was studied the effect of acetic acid concentration and extraction time on the collagen quality of black tilapia leather. Black tilapia leather processed into collagen as an alternative to increasing value-added of fisheries industry waste. Collagen of black tilapia was extracted by the treatment of acetic acid molarity, each: 0.25 M, 0.50 M, and 0.75 M (A factor) and extraction time of 16 and 48 hours (B factor). Based on the analysis of variance, is known that the interaction of those treatments (AB) didn’t significantly effect on the yield (p>0.05). Collagen extraction of tilapia leather with 0.75 M of acetic acid at 16 hours, produces the greatest yield (5.97%), with denaturation temperature is 35.75oC, and quantitative composition of glisine, alanine, and glutamic amino acids were: 5395.82 ppm (52.99%), 2979.15 ppm (22.08%), and 1684.42 ppm (7.45%). Based on the analysis of SDS-PAGE, is known that the collagen contained were α component and β component, so that collagen of tilapia leather has type I collagen.

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Repairing the ruptured annular fibrosus by using type I collagen combined with citric acid, EDC and NHS: an in vivo study

European Spine Journal ◽

10.1007/s00586-016-4898-1 ◽

2016 ◽

Vol 26 (3) ◽

pp. 884-893 ◽

Cited By ~ 5

Author(s):

Yan Wang ◽

Xiaoting Wang ◽

Jin Shang ◽

Huan Liu ◽

Yi Yuan ◽

...

Keyword(s):

Citric Acid ◽

Type I Collagen ◽

In Vivo Study ◽

Type I

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Optimization and Preliminary Physicochemical Characterization of Pectin Extraction from Watermelon Rind (Citrullus lanatus) with Citric Acid

International Journal of Food Science ◽

10.1155/2022/3068829 ◽

2022 ◽

Vol 2022 ◽

pp. 1-10

Author(s):

José Pérez ◽

Karina Gómez ◽

Lorena Vega

Keyword(s):

Citric Acid ◽

High Purity ◽

Acid Content ◽

Physicochemical Characterization ◽

Extraction Time ◽

Significant Variable ◽

Optimal Conditions ◽

Degree Of Esterification ◽

Solid Ratio ◽

Watermelon Rind

Watermelon rind was used for the pectin extraction with citric acid as the extractant solvent. The effects of pH (2.0-3.0), extraction time (45-75 min), and liquid-solid ratio (10 : 1 to 40 : 1 mL/g) on the pectin yield, degree of esterification, methoxyl content, and anhydrouronic acid content were investigated using Box-Behnken surface response experimental design. The pH was the most significant variable for the pectin yield and properties. The responses optimized separately showed different optimal conditions for each one of the variables studied in this work. Therefore, the desirability function was used to determine the sole theoretical optimum for the highest pectin yield and highest anhydrouronic acid content, which was found to be pH of 2.0, extraction time of 62.31 min, and liquid-solid ratio of 35.07 mL/g. Under this optimal condition, the pectin yield, degree of esterification, methoxyl content, and anhydrouronic acid content were 24.30%, 73.30%, 10.45%, and 81.33%, respectively. At optimal conditions, watermelon rind pectin can be classified as high methoxyl and rapid-set pectin with high quality and high purity. Practical Applications. This study evaluated the pectin extraction from watermelon rind and carried out an optimization of multiple responses as a function of pH, time, and liquid-solid ratio to obtain the best preliminary quality parameters (pectin yield and anhydrouronic acid content). The results revealed that watermelon rind waste can be an inexpensive source to obtain good pectin quality and high purity. According to the chemical characterization and physicochemical properties studied, the extracted pectin from watermelon rind would have a high potential to be used in food industry.

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Optimization and Physicochemical Characterization of Pectin Extraction from Watermelon Rind (Citrullus lanatus) with Citric Acid

10.21203/rs.3.rs-268492/v1 ◽

2021 ◽

Author(s):

Jose Perez ◽

Karina Gomez ◽

Lorena Vega

Keyword(s):

Citric Acid ◽

Acid Content ◽

Citrullus Lanatus ◽

Physicochemical Characterization ◽

Extraction Time ◽

Significant Variable ◽

Optimal Conditions ◽

Degree Of Esterification ◽

Solid Ratio ◽

Watermelon Rind

Abstract Watermelon rind was used for the pectin extraction with citric acid as the extractant solvent. The effects of pH (2.0-3.0), extraction time (45-75 min) and liquid-solid ratio (1:10-1:40 g/ml) on the pectin yield, degree of esterification, methoxyl content and anhydrouronic acid content were investigated using Box-Behnken surface response experimental design. The pH was the most significant variable for the pectin yield and properties. The responses optimized separately showed different optimal conditions for each of the variables studied in this work. Therefore, the desirability function was used to determine the sole theoretical optimum for the highest pectin yield and highest anhydrouronic acid content, which was found to be: pH of 2.0, extraction time of 62.31 min and liquid-solid ratio of 35.07 g/mL. Under this optimal condition, the pectin yield, degree of esterification, methoxyl content and anhydrouronic acid content were 24.30%, 73.30%, 10.45% and 81.33%, respectively. At optimal conditions, watermelon rind pectin can be classified as high methoxyl and rapid-set pectin with high quality and high-purity.

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Extraction Optimization and Characterization of Collagen from Yellow Pike Conger Swimbladder with Acid-Hydro-Exctraction Method

Jurnal Pengolahan Hasil Perikanan Indonesia ◽

10.17844/jphpi.v19i2.13223 ◽

2016 ◽

Vol 19 (2) ◽

pp. 156

Author(s):

Fernandy Djailani ◽

Wini Trilaksani ◽

Tati |Nurhayati

Keyword(s):

Amino Acid ◽

Acid Content ◽

Type I Collagen ◽

Amino Acid Content ◽

Extraction Time ◽

Yield Response ◽

Type I ◽

Alternative Source ◽

Extraction Optimization ◽

Ft Ir

Swim bladder is one of marine potential byproducts for alternative source of collagen. This study aimed to optimize hydro-extraction and characterized collagen. Extraction optimization of collagen was determined using Box-behnken design response surface method with three variables: CH3 COOH concentration, soaking time and extraction time to yield response. Hydro-extraction collagen was characterization based on the amino acid content, SDS-PAGE, FT-IR and DSC. Acording to the result, the concentration had significantly influence yield. Optimum extraction conditions were variable combinations of acetic acid concentration of 0.1 M, for 1 h and hydro-extraction time of 1 h to produce the highest yield 63.35%. collagen was classified as type I collagen by amino acid content, electrophoresis patterns and fourier transform infrared (FTIR) spectra. The glass transition of collagen was 67.23o C, showed high thermal stability that can be applied to the cosmetics industry and nutraceutical.

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Collagen fibrillogenesis in vitro: interaction of types I and V collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142670 ◽

1986 ◽

Vol 44 ◽

pp. 210-211

Author(s):

Arthur J. Wasserman ◽

Kathy C. Kloos ◽

David E. Birk

Keyword(s):

Type I Collagen ◽

Corneal Stroma ◽

Minor Component ◽

Homogeneous Distribution ◽

Type I ◽

Type V Collagen ◽

Fibril Morphology ◽

Type V ◽

In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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