超声振幅对梭鲈皮肤胶原蛋白产量和性质的影响

Q4 Agricultural and Biological Sciences Journal of Tropical Life Science Pub Date : 2023-05-25 DOI:10.11594/jtls.13.02.03
U. Razali, Ainaa Juraimy, Y. Jusoh, D. Dailin, H. Ya’akob, Noorazwani Zainool, D. Zaidel
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引用次数: 0

摘要

鲱鱼皮是鱼类加工业的副产品,已经显示出作为替代胶原蛋白来源的潜力。然而,常用的酸萃取法生产胶原蛋白,产率低,需要较长的时间,而且不环保。因此,采用更环保的技术,如超声波,来改进传统的提取过程正在出现。本研究旨在探讨不同超声振幅对梭鱼皮肤胶原蛋白恢复的影响。评价所得胶原蛋白的蛋白质、羟脯氨酸和水分含量、颜色、分子量分布和红外光谱。超声辅助提取(UAE)在40 (UAE40), 60 (UAE60)和80 (UAE80) %的振幅下提取20 min。为了进行比较,乙酸提取也得到酸溶性胶原(ASC)。与ASC相比,UAE提高了梭鱼皮肤胶原蛋白的产量(p<0.05),其中UAE80的产量增加了7倍。超声振幅的增加使产率显著提高,但羟脯氨酸含量降低,表明胶原质的降低。此外,提取的胶原蛋白的蛋白质含量和SDS-PAGE图谱显示,阿联酋促进了蛋白质的降解。FTIR光谱表明,尽管波数略有变化,但在存在酰胺A、B、I、II和III的情况下,UAE对三螺旋结构没有不利影响。α1、α2和ß-链在所有样品中均存在,但能带强度随振幅的增大而减小。综上所述,在适当的条件下,UAE可以在不影响胶原结构的情况下提高提取率。
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Effect of Ultrasonic Amplitude on the Yield and Properties of Barramundi (Lates calcarifer) Skin Collagen
Barramundi skin, a by-product of the fish processing industry, has shown potential as an alternative collagen source. However, the commonly used acid extraction method to produce collagen rendered a low yield requires a lengthy time and is not environmentally friendly. As a result, the adoption of greener technology, such as ultrasound, to improve the conventional extraction process is emerging. This study aimed to investigate the effect of different ultrasonication amplitudes on collagen recovery from barramundi skin. The resulting collagens were evaluated for their protein, hydroxyproline and moisture content, colour, molecular weight distribution, and FTIR spectra. Ultrasound-assisted extraction (UAE) was performed at 40 (UAE40), 60 (UAE60) and 80 (UAE80) % amplitude for 20 min. For comparison, acetic acid extraction was also carried out to produce acid-soluble collagen (ASC). UAE increased the yield (p<0.05) of collagen from barramundi skin, with UAE80 exhibiting a 7-fold increment compared to ASC. Increasing the ultrasonic amplitude increased the yield considerably but decreased the hydroxyproline content, indicating a reduction in collagen quality. Furthermore, the protein content and SDS-PAGE profile of the extracted collagens revealed that UAE promoted protein degradation. FTIR spectra indicated that despite slightly varying wavenumbers, no detrimental effect on the triple helical structure was seen following UAE with the presence of amides A, B, I, II, and III. Also, the α1, α2 and ß-chains were found in all samples, although the band intensity reduced as the amplitude increased. In conclusion, given the right conditions, UAE could improve the extraction yield without influencing the collagen structure.
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来源期刊
Journal of Tropical Life Science
Journal of Tropical Life Science Environmental Science-Ecology
CiteScore
1.00
自引率
0.00%
发文量
46
审稿时长
12 weeks
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