Chemical compositions of the roes from skipjack, tongol and bonito

Intarasirisawat, Rossawan; Benjakul, Soottawat; Visessanguan, Wonnop

doi:10.1016/j.foodchem.2010.07.076

Cited by 75 publications

(65 citation statements)

References 28 publications

(64 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Heu et al (2006) reported that skipjack and yellowfin tuna roes contained 71.1-71.2 % moisture, 21.4-21.5 % protein, 2.0-2.1 % lipid and 1.9 % ash, and both tuna roes were no difference in proximate compositions. Intarasirisawat et al (2011) reported that three different tuna species (skipjack, tongol and bonito) roes contained 72. 17-73.03 % moisture, 18.16-20.15 % protein, 3.39-5.68 % lipid and 1.79-2.10 % ash.…”

Section: Proximate Compositionmentioning

confidence: 99%

“…Among byproducts, roes are highly nutritious material rich in essential fatty acids and amino acids (Heu et al 2006;Narsing Rao et al 2012b). Fish roes are produced in large quantities during the spawning seasons, which constitute about 1-3 % of the weight of fish (Chalamaiah et al 2013;Klomklao et al 2013;Intarasirisawat et al 2011). Currently roe obtained from fish such as salmon, cod, and pollock have a potential commercial market, especially they have a higher demand in Asian countries (Sathivel et al 2009).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

et al. 2016

View full text Add to dashboard Cite

Roe is the term used to describe fish eggs (oocytes) gathered in skeins and is one of the most valuable food products from fishery sources. Thus, means of processing are required to convert the underutilized yellowfin tuna roes (YTR) into more marketable and acceptable forms as protein concentrate. Roe protein concentrates (RPCs) were prepared by cooking condition (boil-dried concentrate, BDC and steam-dried concentrate, SDC, respectively) and un-cooking condition (freeze-dried concentrate, FDC) from yellowfin tuna roe. The yield of RPCs was in the range from 22.2 to 25.3 g/100 g of roe. RPCs contained protein (72.3-77.3 %), moisture (4.3-5.6 %), lipid (10.6-11.3 %) and ash (4.3-5.7 %) as the major constituents. The prominent amino acids of RPCs were aspartic acid, 8.7-9.2, glutamic acid, 13.1-13.2, and leucine, 8.5-8.6 g/100 g of protein.Major differences were not observed in each of the amino acid. K, S, Na, and P as minerals were the major elements in RPCs. No difference noted in sodium dodecyl sulfate polyacrylamide gel electrophoresis protein band (15-100 K) possibly representing partial hydrolysis of myosin. Therefore, RPCs from YTR could be use potential protein ingredient for human food and animal feeds.

show abstract

Section: Proximate Compositionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

et al. 2016

View full text Add to dashboard Cite

show abstract

“…, (Joe and Jo, 1993) (Joe, 1991) , shelf-life (Kim, 1996), (Park et al, 1983), (Kim et al, 1988), (Shimada and Ogura, 1990), (Eun et al, 1994) (Jeong et al, 2000) , (Heu et al, 2006) (Intarasirisawat et al, 2011) .…”

mentioning

confidence: 99%

Chromatographic Fractionation of Protease Inhibitors from Fish Eggs

Kim¹,

Kim²,

Kim³

et al. 2013

Korean Journal of Fisheries and Aquatic Sciences

View full text Add to dashboard Cite

A protease inhibitor from fish eggs was fractionated using chromatographic methods. The fractionation efficiency was evaluated in terms of specific inhibitory activity (SIA, U/mg), purity (fold), total inhibitory activity (TIA, U), and recovery (%). The protease inhibitor (PI) from egg extracts of skipjack tuna (ST Katsuwonus pelamis), yellowfin tuna (YT Thunnus albacares) and Alaska pollock (AP Theragra chalcogramma) was fractionated using Sephadex G-50 gel filtration and DEAE-Sepharose CL-6B anion exchange chromatography based on protein size exclusion and net charge, respectively. Fractions exhibiting strong inhibitory activity were contained in the 30-50 kDa fraction on gel filtration and in the range of 0.4-0.7 M NaCl gradient fraction on anion exchange chromatography. The respective TIA and percent recovery of the fraction obtained with gel filtration toward trypsin and Nα-benzoyl-L-arginine-pnitroanilide (BAPNA) were 2,758.7 U and 29.6% for ST, 1,005.5 U and 25.6% for YT, and 1,267.5 U and 26.0% for AP. Gel filtration chromatography was more effective at fractionating PI than using ion exchange chromatography. These results suggest that fish eggs act as serine protease inhibitors and might be useful for protease inhibition in foodstuffs.

show abstract

“…Fish roe are considered as the important source for the bioactive compounds, which exhibit antioxidant, antibacterial and immunomodulatory activities. Intarasirisawat et al (2011) reported that fish roe is rich in polyunsaturated fatty acids (PUFAs). Fish egg protein hydrolysates showed fat adsorption capacity, foam capacity and emulsifying capacity (Chalamaiah et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Serine protease inhibitors from squid ovary: extraction and its effect on proteolysis and gel properties of surimi

Singh

Benjakul

2016

J Food Sci Technol

Self Cite

View full text Add to dashboard Cite

Serine protease inhibitors from squid ovary (SOSPI) were extracted using different extraction media and conditions. Optimal condition included 0.45 M NaCl for 1 h. After heat treatment at 70°C for 10 min, the highest specific activity was obtained. Based on Sephadex G-75 gel filtration and activity staining, the major SOSPIs were present as monomer with molecular weight of 9.10 and 10.27 kDa. Impact of SOSPI on autolysis of bigeye snapper surimi was studied. Myosin heavy chain was more retained with coincidentally lower trichloroacetic acidsoluble peptide content as the level of SOSPI increased. When SOSPI at various levels (0.5-3%) was added into surimi, the highest breaking force of both kamaboko and modori gels containing 1% SOSPI was obtained. However, SOSPI had no effect on deformation of kamaboko gel but slightly increased the deformation of modori gel. SOSPI increased water holding capacity of both kamaboko and modori gels in a dose dependent manner, as indicated by the lowered expressible moisture content. SOSPI had no effect on the whiteness of both gels. Thus SOSPI can be used as the protein additive in surimi for increasing breaking force.

show abstract

Chemical compositions of the roes from skipjack, tongol and bonito

Cited by 75 publications

References 28 publications

Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

Chromatographic Fractionation of Protease Inhibitors from Fish Eggs

Serine protease inhibitors from squid ovary: extraction and its effect on proteolysis and gel properties of surimi

Contact Info

Product

Resources

About