The effect of fish bone collagens in improving food quality

Y. S. Darmanto, T. W. Agustini, F. Swastawati, I. Al Bulushi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The aim of this study was to evaluate the effect of addition of 6% collagen extracted from various sources of fish bones on the quality of myofibril proteins of fish. For this purpose, fish bones were collected from 9 different fish species: seawater catfish (Arius thalasinus), threadfin bream (Nemipterus nematophorus), stingrayfish (Dasyatis sephen), big eye snapper (Lutjanus lutjanus), catfish (Clarias batrachus), shark (Charcarius sp), eastern little tuna (Euthynnus affinis), lizardfish (Saurida tumbil) and purple-spotted bigeye (Priacanthus tayenus). Quality of myofibril was evaluated for its water sorption isotherm, Ca-ATPase activity, water holding capacity, gel strength, folding test and viscosity of protein, as well as proximate composition, phosphorus and calcium contents as supporting quality parameters. The result showed that the effect of collagen addition on the phosphorus and calcium contents in myofibril proteins varies according to fish sources species. The addition of collagen can also retard the decrease of Ca-ATPase activity, viscosity, gel strength, folding test and water holding capacity in myofibril proteins. High value of gel strength, water holding capacity and folding test shows a high quality of myofibril protein-based product, especially for collagen added from snapper collagen with the value of 1436.2 gr/cm, 41.2 ± 0.04, A, respectively and threadfin bream collagen with the value of 1596.10 gr/cm, 52.27 ± 0.02, A, respectively. The addition of fish bone collagens did not show significant difference in water sorption isotherm profile of myofibril protein, but all collagens has an effect on retarding the denaturation rate of myofibril protein. This research delivered a conclusion that collagen extracted from various source of fish bones have influences on food quality especially in altering the rate of protein denaturation.

Original languageEnglish
Pages (from-to)891-896
Number of pages6
JournalInternational Food Research Journal
Volume21
Issue number3
Publication statusPublished - 2014

Fingerprint

Food Quality
food quality
Myofibrils
myofibrils
collagen
Fishes
Collagen
bones
Bone and Bones
fish
Catfishes
gel strength
Water
water holding capacity
Polynemidae
proteins
Lutjanus
Proteins
snapper
Ca2-transporting ATPase

Keywords

  • Ca-ATPase activity
  • Collagen
  • Fish bones
  • Myofibril protein

ASJC Scopus subject areas

  • Food Science

Cite this

Darmanto, Y. S., Agustini, T. W., Swastawati, F., & Al Bulushi, I. (2014). The effect of fish bone collagens in improving food quality. International Food Research Journal, 21(3), 891-896.

The effect of fish bone collagens in improving food quality. / Darmanto, Y. S.; Agustini, T. W.; Swastawati, F.; Al Bulushi, I.

In: International Food Research Journal, Vol. 21, No. 3, 2014, p. 891-896.

Research output: Contribution to journalArticle

Darmanto, YS, Agustini, TW, Swastawati, F & Al Bulushi, I 2014, 'The effect of fish bone collagens in improving food quality', International Food Research Journal, vol. 21, no. 3, pp. 891-896.
Darmanto, Y. S. ; Agustini, T. W. ; Swastawati, F. ; Al Bulushi, I. / The effect of fish bone collagens in improving food quality. In: International Food Research Journal. 2014 ; Vol. 21, No. 3. pp. 891-896.
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AB - The aim of this study was to evaluate the effect of addition of 6% collagen extracted from various sources of fish bones on the quality of myofibril proteins of fish. For this purpose, fish bones were collected from 9 different fish species: seawater catfish (Arius thalasinus), threadfin bream (Nemipterus nematophorus), stingrayfish (Dasyatis sephen), big eye snapper (Lutjanus lutjanus), catfish (Clarias batrachus), shark (Charcarius sp), eastern little tuna (Euthynnus affinis), lizardfish (Saurida tumbil) and purple-spotted bigeye (Priacanthus tayenus). Quality of myofibril was evaluated for its water sorption isotherm, Ca-ATPase activity, water holding capacity, gel strength, folding test and viscosity of protein, as well as proximate composition, phosphorus and calcium contents as supporting quality parameters. The result showed that the effect of collagen addition on the phosphorus and calcium contents in myofibril proteins varies according to fish sources species. The addition of collagen can also retard the decrease of Ca-ATPase activity, viscosity, gel strength, folding test and water holding capacity in myofibril proteins. High value of gel strength, water holding capacity and folding test shows a high quality of myofibril protein-based product, especially for collagen added from snapper collagen with the value of 1436.2 gr/cm, 41.2 ± 0.04, A, respectively and threadfin bream collagen with the value of 1596.10 gr/cm, 52.27 ± 0.02, A, respectively. The addition of fish bone collagens did not show significant difference in water sorption isotherm profile of myofibril protein, but all collagens has an effect on retarding the denaturation rate of myofibril protein. This research delivered a conclusion that collagen extracted from various source of fish bones have influences on food quality especially in altering the rate of protein denaturation.

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