การสกัดและการจำแนกคุณสมบัติของคอลลาเจนและเจลาตินจากหนังและกระดูกปลาตาหวาน

Thesis (M.Sc., Food Technology)--Prince of Songkla University, 200

Characteristics of collagen from the skin of clown featherback (Chitala ornata)

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of clown featherback (Chitala ornata) were isolated and characterised. Yields of ASC and PSC were 27.64 and 44.63% (dry weight basis) with total collagen recovery of 82.08%. Both collagens contained glycine as the major amino acid with relatively high content of proline, hydroxyproline and glutamic acid/glutamine. Nevertheless, they had the low content of cysteine, histidine and tryrosine. The collagen was characterised as type I, comprising (1)(2)2-heterotrimer. Pepsin-aided process did not affect triple-helical structure of PSC as determined by FTIR spectra. Thermal transition temperature of ASC (36.28 degrees C) was slightly higher than that of PSC (35.23 degrees C). However, no differences in isoelectric point (5.54-5.68) between ASC and PSC were observed. Therefore, collagen from the skin of clown featherback could be successfully extracted for further applications

Characteristics of Collagen from Rohu (Labeo rohita) Skin

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196-202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (1)(2)2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The T-max value of ASC and PSC was 36.40 and 35.48 degrees C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively

Molecular, Structural, and Rheological Characterization of Camel Skin Gelatin Extracted Using Different Pretreatment Conditions

Optimum conditions for high-quality gelatin recovery from camel skin and its molecular, structural, and rheological characterization were carried out in this study. Increased yield and gel strength were recorded, with an increase in camel skin pretreatment times of 6 to 42 h and 0.50 and 0.75 M-NaOH. Gelatin from skin pretreated with 0.75 and 0.5 M-NaOH for 42 h showed the highest yield (22.60%) and gel strength (365.5 g), respectively. Structural characterization by Fourier transformation infrared spectra, X-ray diffraction, and nuclear magnetic resonance indicated that all gelatins possessed major peaks in the amide region, and diffraction peaks around 22° were basically amorphous. The temperatures for gelling and melting ranged from 20.9 °C to 25.8 °C and 27.34 °C to 30.49 °C. Microstructure revealed loose network with more voids in gelatin from skin pretreated with 0.5 and 0.75 M-NaOH for 6 h, while a highly cross-linked network and less voids were observed in those pretreated with 0.75 M-NaOH for 24 h and 0.5 M-NaOH for 42 h. The results reveal that great potential exists in producing halal gelatin with excellent quality and functionality from camel skin

Characteristics of Collagen from Rohu ( Labeo rohita

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196-202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (1)(2)2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The T-max value of ASC and PSC was 36.40 and 35.48 degrees C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively