Properties study of fish collagen and gelatin blend for high-temperature food applications

Sustainable food production is becoming a necessity due to the overwhelming demand for global resources. In meeting these demands, an equivalent amount of waste is being generated at the same time. In aquaculture, for instance, staggering amounts of fisheries wastes – primarily skins, were left accu...

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Main Author: Chay, Jie Cheng
Other Authors: Tan Lay Poh
Format: Thesis-Master by Research
Language:English
Published: Nanyang Technological University 2022
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Online Access:https://hdl.handle.net/10356/163018
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1630182022-12-07T06:25:18Z Properties study of fish collagen and gelatin blend for high-temperature food applications Chay, Jie Cheng Tan Lay Poh School of Materials Science and Engineering LPTan@ntu.edu.sg Engineering::Materials Sustainable food production is becoming a necessity due to the overwhelming demand for global resources. In meeting these demands, an equivalent amount of waste is being generated at the same time. In aquaculture, for instance, staggering amounts of fisheries wastes – primarily skins, were left accumulated in the processing industries. These wastes contain valuable bioresources that can be contributed back to the supply chain for functional food developments. This study adopts the concept of waste valorization to recover collagen-I from Barramundi fish skins. A remarkable collagen yield of 74.57 % was obtained by acetic acid solubilization, with a modest pretreatment concentration responsible for the increased yield. FTIR analysis reveals its intact triple-helical structure, against gelatin from subsequent extraction. At present, sustainable utilization of fish collagen has been limited by its ease of denaturation. Especially in the field of food applications, where extreme heating conditions are often involved. This study may be the first to formulate an edible collagen-based gel, that is stable for boiling at 100 ˚C. MTGase was involved to crosslink collagen with gelatin enzymatically, for increased crosslinking density. Synergistically, the collagen reinforces gelatin gels with excellent chewiness from 5.85 to 36.51 kPa, which is an important texture indicator for meat and fish products. The findings elucidated that textural properties are closely dependent on the collagen helices, rather than the crosslinking density that contributed to enhanced thermal stability. Overall, the blended gel demonstrates improved viability for high-temperature food applications, along with textures useful for functional food developments. Master of Engineering 2022-11-22T04:54:51Z 2022-11-22T04:54:51Z 2022 Thesis-Master by Research Chay, J. C. (2022). Properties study of fish collagen and gelatin blend for high-temperature food applications. Master's thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/163018 https://hdl.handle.net/10356/163018 10.32657/10356/163018 en This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0). application/pdf Nanyang Technological University
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Materials
spellingShingle Engineering::Materials
Chay, Jie Cheng
Properties study of fish collagen and gelatin blend for high-temperature food applications
description Sustainable food production is becoming a necessity due to the overwhelming demand for global resources. In meeting these demands, an equivalent amount of waste is being generated at the same time. In aquaculture, for instance, staggering amounts of fisheries wastes – primarily skins, were left accumulated in the processing industries. These wastes contain valuable bioresources that can be contributed back to the supply chain for functional food developments. This study adopts the concept of waste valorization to recover collagen-I from Barramundi fish skins. A remarkable collagen yield of 74.57 % was obtained by acetic acid solubilization, with a modest pretreatment concentration responsible for the increased yield. FTIR analysis reveals its intact triple-helical structure, against gelatin from subsequent extraction. At present, sustainable utilization of fish collagen has been limited by its ease of denaturation. Especially in the field of food applications, where extreme heating conditions are often involved. This study may be the first to formulate an edible collagen-based gel, that is stable for boiling at 100 ˚C. MTGase was involved to crosslink collagen with gelatin enzymatically, for increased crosslinking density. Synergistically, the collagen reinforces gelatin gels with excellent chewiness from 5.85 to 36.51 kPa, which is an important texture indicator for meat and fish products. The findings elucidated that textural properties are closely dependent on the collagen helices, rather than the crosslinking density that contributed to enhanced thermal stability. Overall, the blended gel demonstrates improved viability for high-temperature food applications, along with textures useful for functional food developments.
author2 Tan Lay Poh
author_facet Tan Lay Poh
Chay, Jie Cheng
format Thesis-Master by Research
author Chay, Jie Cheng
author_sort Chay, Jie Cheng
title Properties study of fish collagen and gelatin blend for high-temperature food applications
title_short Properties study of fish collagen and gelatin blend for high-temperature food applications
title_full Properties study of fish collagen and gelatin blend for high-temperature food applications
title_fullStr Properties study of fish collagen and gelatin blend for high-temperature food applications
title_full_unstemmed Properties study of fish collagen and gelatin blend for high-temperature food applications
title_sort properties study of fish collagen and gelatin blend for high-temperature food applications
publisher Nanyang Technological University
publishDate 2022
url https://hdl.handle.net/10356/163018
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