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2019 | 28 | 4 |

Tytuł artykułu

Extraction and properties of acid-soluble collagen and pepsin-soluble collagen from silver carp (Hypophthalmichthys molitrix) scales: prerequisite information for fishery processing waste reuse

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
As a waste of the fish processing industry, scales cause the disposal of large amounts of solid waste into the environment. How to turn such waste into a useful product is an important issue. In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from silver carp (Hypophthalmichthys molitrix) scales using a new acid-enzyme combined method. The results showed that the extraction yields of ASC and PSC were 5.09% and 12.06%, respectively. Then amino acid analysis, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) and ultra-sensitive differential scanning calorimetry (US-DSC) were used to study their composition, properties and structure. Amino acid analysis indicated that ASC and PSC were type I collagens with 34% glycine and 20% imino acid (Pro and Hyp). The results of SDS-PAGE and FT-IR analysis showed that ASC and PSC were similar to those of the standard type I collagen. CD indicated that the triple helical structure of both ASC and PSC were still retained. And the transition from triple helix to random coil of ASC and PSC were 34.26ºC and 34.47ºC, respectively. For the first time, the collagen yields of silver carp scales were calculated. Meanwhile, their composition, properties and structure were characterized. These results may offer theoretical support for the development of silver carp scales related to reusing technology to control waste.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

28

Numer

4

Opis fizyczny

p.2923-2930,fig.,ref.

Twórcy

autor
  • National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, China
autor
  • National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, China
autor
  • National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, China
autor
  • National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, China
  • Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu, China

Bibliografia

  • 1. KITTIPHATTANABAWON P., BENJAKUL S., VISESSANGUAN W., NAGAI T., TANAKA M. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem. 89 (3), 363, 2005.
  • 2. SINTHUSAMRAN S., BENJAKUL S., KISHIMURA H. Comparative study on molecular characteristics of acid soluble collagens from skin and swim bladder of seabass (Lates calcarifer). Food Chem. 138 (4), 2435, 2013.
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  • 15. WU J.C., GAO Y.P., ZHANG J.W., WANG Y., CHEN W.Y. chrome complexes in rewetting and neutralizing effluents and hints for recycling post-tanning wet-process effluent. Pol. J. Environ. Stud. 27 (3), 1, 2018.
  • 16. SARKAR H.S., DAS S., RISSANEN K., SAHOO P. First chemosensor for selective detection and quantification of l-4-hydroxyproline in collagen and other bio samples. Analytical Chemistry. 89 (24), 13054, 2017.
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  • 21. WANG Z.B., WANG L., LIN S.M., LIANG Q.F., SHI Z.J., XU J.M., MA H.L. Isolation and characterization of collagen from the muscle of Amur sturgeon (Acipenser schrenckii). Biotechnology and Bioprocess Engineering. 19 (5), 935, 2014.
  • 22. ALI M.M., BENJAKUL S., PRODPRAN T., KISHIMURA H. Extraction and characterisation of collagen from the skin of golden carp (Probarbus jullieni), a processing byproduct. Waste and Biomass Valorization. 9 (5), 783, 2018.
  • 23. NALINANON S., BENJAKUL S., KISHIMURA H. Collagens from the skin of arabesque greenling (Pleurogrammus azonus) solubilised with the aid of acetic acid and pepsin from albacore tuna (Thunnus alalunga) stomach. J. Sci Food Agr. 90 (9), 1492, 2010.
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  • 27. Wegener H., Paulsen H., Seeger K. The cysteinerich region of type vii collagen is a cystine knot with a new topology*. Journal of Biological Chemistry. 289 (8), 4861, 2014.
  • 28. Motooka D., Kawahara K., Nakamura S., Doi M., Nishi Y., Nishiuchi Y., Kang Y.K., Nakazawa T., Uchi yama S., Yoshida T., Ohkubo T., Koba yashi Y. The triple helical structure and stability of collagen model peptide with 4(s)-hydroxyprolyl-pro-gly units. Biopolymers. 98 (2), 111, 2012.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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