Paper Titles

Antimicrobial Activity of Myrica rubra Essential Oil against Five Pathogenic Food-Borne Bacteria
p.1646

The Rheological Properties of κ-Carrageenan-Konjac Gum Mixed Gel
p.1652

Effects of Lactic Acid Bacteria on Nitrite Degradation during Pickle Fermentation
p.1656

An Investigation on Urban Office Workers' Cognition on Food Safety when Eating Out
p.1661

Effects of Heat Treatment on Water Soluble Compounds of Grass Carp
p.1665

Extruder Responses, Textural Properties and Color of Meat Analogs Made by High Moisture Soybean Residue and Soy Protein Isolate
p.1670

Preliminary Analysis of Bacterial Flora in Turbot Scophthalmus maximus Cultured in Deep Well Seawater
p.1677

Isolation and Characteristics of Cholesterol-Lowering L. casei subsp. casei Strain GL-03 Isolated from Cheese
p.1681

Characterization of Tomato Fruit LeRIN Gene Application Virus-Induced Gene Silencing Technology
p.1685

HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 781-784Effects of Heat Treatment on Water Soluble...

Effects of Heat Treatment on Water Soluble Compounds of Grass Carp

Article Preview

Abstract:

Experiment was studied on water soluble compounds of grass carp (dorsal meat) with different heat treatment. The result showed that different heat treatment can cause the difference of water soluble compounds. IMP is one of degradation products of ATP, the content would increase with ATP degradation in a certain period. K value of fresh sample was 1.83%, it had no obvious difference after in the refrigerator of-20°C for 48 hours, but it increased compared with fresh sample when heated and reheated. In the dorsal meat, the contents of glycine (Gly) alanine (Ala) and histidine (His) were higher than others. The contents of total free amino acids (TFAA) contents reached maximum when reheated for fresh sample. The contents of TFAA in grass carp had no obvious regularity changes with different heat treatment.

You might also be interested in these eBooks

Advances in Chemical Engineering III

Info:

Periodical:

Advanced Materials Research (Volumes 781-784)

Pages:

1665-1669

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.781-784.1665

Citation:

Cite this paper

Online since:

September 2013

Authors:

Qing Yun Chen, Wen Zheng Shi*, Jin Qing Wan, Zhi He Wang

Keywords:

Free Amino Acid, Grass Carp, Heat Treatment, k-Value, Water Soluble Compounds

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

© 2013 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

* - Corresponding Author

[32] 58±1. 82a.

[1] 19±0. 35ef.

98±0. 01f.

[9] 27±0. 58bc.

[9] 04±0. 79c.

[5] 67±0. 07d ADP.

[10] 97±0. 33.

[26] 15±1. 26.

[12] 50±0. 69.

[4] 07±0. 35.

[21] 22±1. 91.

[30] 12±0. 35 AMP.

[4] 60±0. 23.

[6] 02±0. 21.

[6] 07±0. 26.

[5] 20±0. 88.

[3] 95±0. 38.

[4] 51±0. 01 Hx.

41±0. 06.

[1] 09±0. 07.

95±0. 01.

82±0. 01.

50±0. 07.

59±0. 09 HxR.

[2] 49±0. 19.

[23] 08±0. 52.

[15] 78±1. 58.

[2] 17±0. 01.

[4] 43±0. 53.

[4] 53±0. 41 K.

[1] 83.

[12] 87.

[10] 52.

[1] 84.

[3] 13.

[3] 13 Note: Ⅰ-Fresh sample, Ⅱ-Cooked fresh sample, Ⅲ-Reheated sample of placed 6h after cooked, Ⅳ-Frozen sample of two days, Ⅴ-Cooked sample of frozen fish, Ⅵ-Reheated sample of placed 6h after cooked frozen fish. Different letter in group means significant difference(p＜0. 05）. Fig. 2 Comparison of K-value K-value is a ratio of sum of HxR and Hx to the sum of ATP-related compounds. By calculating, K value of grass carp in different treatment is shown in fig. 2. In the fig. 2, K value of grass carp is not same under different heat treatment mode. It showed a trend of falling after rising according to the processing order of from Ⅰ to Ⅵ. K-value was 1. 83% in fresh sample, and had no obvious difference after in the refrigerator of -20℃ for 48 hours, but it increased compared with fresh sample when heated and reheated, and reached maximum at the first cooked for fresh sample. This is mainly because in heating process, ATP will decrease with its own decomposition and loss of juice. But ATP and its associated contents have different solubility in water, therefore the lost amount of nucleotides along with water loss is different. This impact caused the fluctu ation of K value. Fig. 3 is the chromatogram containing 16 free amino acids standards, including Asp, Thr, Ser, Glu, Gly, Ala, Cys, Val, Met, Ile, Leu, Tyr, Phe, Lys, His, Arg. Pro is shown at another channel. Free amino acid is one of the main components of flavor substances, when some free amino acids exist with high enough concentrations in fish, they can contribute to the flavor independently of the other components[9]. According to the associated report, Gly contributes to the sweet taste of fish [10], Lys produces sweet bitter, His causes the feature of rise wisps[11]. Leu and Ile is bitter amino acids, Met is indispensable ingredient in sea urchin flavor [12]. Free amino acids of Higher contents in grass carp mainly include Thr, Gly, Ala, Ile, Leu, Lys and His, they can reach 2. 8%, 19. 9%, 8. 2%, 1. 7%, 1. 9%, 1. 4%, 49. 8% respectively. But Thr has litter effect on the flavor of fish because of the lower content and higher threshold in grass carp. Tab. 2 Fig. 3 Chromatogram of free amino acids standard substances Tab. 2 The contents of free amino acids in grass carp(μg/g) amino acid type Ⅰ Ⅱ Ⅲ Ⅳ Ⅴ Ⅵ threshold Asp.

[5] 98±0. 53d.

[6] 48±0. 32cd.

[7] 62±0. 32ab.

[8] 38±0. 82a.

[7] 05±0. 07bcd.

[7] 56±0. 22abc.

[30] 00 Thr 121. 46±13. 81c 138. 00±4. 72abc 154. 61±3. 75a 124. 14±7. 82bc.

[89] 46±0. 52de.

[84] 95±1. 32e 2600. 00 Ser.

[67] 56±7. 33a.

[72] 22±2. 27a.

[80] 39±1. 41a.

[64] 78±5. 14abc.

[47] 95±0. 91c.

[48] 94±0. 66bc 1500. 00 Glu.

[14] 27±1. 43cd.

[28] 50±2. 44b.

[36] 15±0. 98a.

[9] 15±0. 47f.

[11] 14±0. 08ef.

[11] 66±0. 08def.

[50] 00 Gly 853. 18±85. 42a 656. 06±35. 93def 733. 78±0. 83bcde 723. 39±46. 38cde 613. 47±13. 87f 626. 96±30. 51ef 1300. 00 Ala 352. 78±31. 10cde 439. 49±10. 90a 491. 02±20. 42a 372. 65±36. 22bcde 326. 93±12. 19e 336. 67±17. 56de 600. 00 Cys.

[41] 05±0. 74b.

[46] 63±2. 05a.

[46] 00±0. 95a.

[44] 88±0. 17ab.

[43] 67±3. 26ab.

[44] 27±0. 20ab Val.

[84] 97±4. 51a.

[83] 41±8. 84a.

[59] 13±0. 79b.

[89] 27±2. 44a.

[83] 44±0. 71a.

[84] 86±0. 59a 400. 00 Met.

[52] 56±1. 42d.

[54] 93±0. 28bcd.

[54] 57±0. 37cd.

[56] 16±1. 64abc.

[57] 28±1. 79abc.

[59] 03±0. 57a 300. 00 Ile.

[74] 01±5. 84abc.

[82] 39±0. 81ab.

[85] 97±0. 87a.

[66] 56±2. 67bc.

[63] 96±1. 05c.

[74] 62±3. 20abc 900. 00 Leu.

[82] 14±5. 94def 108. 52±0. 87b 117. 00±2. 63a.

[83] 02±1. 98cdef.

[79] 37±0. 15f.

[82] 02±0. 44ef 1900. 00 Tyr.

[47] 44±1. 05c.

[55] 79±1. 44a.

[52] 48±1. 41ab.

[49] 72±0. 91bc.

[52] 63±0. 39ab.

[55] 49±2. 60a Phe.

[34] 63±0. 25cd.

[35] 09±0. 49abcd.

[34] 59±1. 09bcd.

[33] 59±1. 93d.

[36] 67±2. 93abcd.

[39] 27±1. 99a 900. 00 Lys.

[58] 90±2. 61e 103. 18±2. 85a 114. 11±1. 81a.

[72] 21±5. 16bcde.

[59] 08±0. 07de.

[60] 27±0. 68cde 500. 00 His 2138. 29±20. 60f 2468. 20±79. 83bcde 2778. 95±76. 83a 2347. 19±0. 21cdef 2227. 28±16. 45ef 2237. 29±22. 82def 200. 00 Arg.

[26] 61±2. 98e.

[39] 96±0. 02a.

[42] 96±1. 66a.

[30] 37±2. 11bcde.

[27] 81±0. 50cde.

[27] 13±0. 60de 500. 00 Pro 236. 26±16. 69a 137. 73±3. 66e 149. 16±0. 45de 234. 60 ±15. 95a 209. 43±2. 64bc 207. 60±0. 53c 300. 00 totle 4292. 09 4556. 58 5038. 49 4410. 06 4036. 62 4088. 59 increase of percentage.

[6] 16.

[17] 39.

[2] 75% -5. 95% -4. 74% Note: Ⅰ- Fresh sample, Ⅱ-Cooked fresh sample, Ⅲ-Reheated sample of placed 6h after cooked, Ⅳ-Frozen sample of two days, Ⅴ-Cooked sample of frozen fish, Ⅵ- Reheated sample of placed 6h after cooked frozen fish. Different letter in group means significant difference (p＜0. 05). Asp-asparaginic, Thr-threonine, Ser-serine, Glu-glutamic, Gly-glycine, Ala-alanine, Cys-cysteine, Val-valine, Met-methionine, Ile-isoleucine, Leu-leucine, Tyr-tyrosine, Phe-phenylalanine, Lys-lysine, His-histidine, Arg-arginine, Pro-proline. TFAA content(μg/g) Fig. 4 Contents of total free amino acids with different treatment showed that free amino acids contents in grass carp with different treatment are different. The content of total free amino acids would increase after frozen 48h, which may be caused by microbial enzyme degradation of proteins [13]. At the same time, aminopeptidase applies to small molecular peptides can also lead to the release of amino acids, increasing the content of FAA [14]. Fig. 4 is the line chart on changes of the total free amino acids contents. TFAA content reached maximum when fresh sample was reheated. For fresh sample, TFAA contents increased by 6. 2% after heated, increased by 17. 4% after reheated, instead reheated after frozen caused the FAA's damage. The change of free amino acids content after heated and reheated is possibly due to thermal degradation of protein and juice loss. Conclusions Freshness with different heat handling in grass carp are different. According to the processing order of from one to six, K value of the three kinds of fish generally present a tendency of falling after rising first, it is possibly due to the interaction between loss of ATP decomposition and juice loss. Free amino acids and total free amino acids with different heat handling are different. They had no obvious regularity. The reason causing this phenomenon are likely to the thermal degradation of protein and juice loss. Acknowledgements The author thank the project supported by the National Science Foundation of China (Grant No. 31171764) and Doctoral foundation of Shanghai Ocean University (Grant No. 110201 ). 1*Corresponding Author: Wenzheng Shi, associate professor, Shanghai Ocean University, E-mail: wzshi@shou. edu. cn. Fund Project: National Science Foundation of China (Grant No. 31171764) and Doctoral Foundation of Shanghai Ocean University (Grant No. 110201). Referents.

[1] Qian Liu, Hong Ji, Shangshun Su, et al. Reservoir Fisheries, 2007, 27(2): 7-8.

[2] Jian Jiang, Xichang Wang, Xiyao Chen. Modern Food Science and Technology, 2006, 22(2): 219-222.

[3] Yokoyama Y, Sakaguchi M, Kawai F, et al. Change in concentration of ATP-related compounds in varioustissues of oyster during ice storage[J]. Nippon Suisan Gakkaishi, 1992, 58(11): 2125-2136.

DOI: 10.2331/suisan.58.2125

[4] Caiwen Dong. Food and Fermentation Industries, 2004, 30(4): 99-103.

[5] Jiechun Deng, Xichang Wang, Yuan Liu. Science and Technology of Food Industry, 2010, 31(3): 106-108.

[6] Saito T, A rai K, M atsugo shi M. A new method for estimating the freshness of fish[J]. Bull Jap SocSci Fish, 1959, 24: 749-750.

[7] Yuexin Shen. Bei jing: China light industry press. (2001).

[8] Xiaoyu Qi, Yan Li, Peigen Zhou. Journal of Fisheries of China, 2001(5)482-484.

[9] Yokoyama Y., SakaguchiM., KawaiF., et al. Changes in concentration of ATP-related compounds in various tissues of oyster during ice storage[J]. Nippon Suisan Gakkaishi, 1992, 58(11): 2125-2136.

DOI: 10.2331/suisan.58.2125

[10] Xiane Ren, Shuihua Zhang. Chinese Condiment, 2003(12): 17-21.

[11] Jie Li, Guobin Zhu. Bei jing: China light industry press. (2001).

[12] Qingxiong Wu, Sikui Qiu. Fishery food[M]. Shanghai: Shanghai science and technology press, 1987: 1-11, 125-129.

[13] Jingke Liu, Shenhua Zhang, Siming Zhao. Journal of Huazhong Agricultural University, (2009).

[14] Yoshio Nishimura, Takahiko Satoh, et al. Synthesis and activity of 1-N-iminosugar inhibitors, siastatin B analogues for α-N-acetylgalactosaminidase and β-N-acetylglucosaminidase. Bioorganic&Medicinal Chemistry, Volume4, Issue1, January1996, Page91-96.

DOI: 10.1016/0968-0896(95)00166-2