Effects of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage

Chow, Chau Jen; Yang, Jing Iong; Lee, Pei Fen; Ochiai, Yoshihiro

doi:10.1007/s12562-009-0168-z

Cited by 23 publications

(19 citation statements)

References 47 publications

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“…The cryoprotectant mixture used in this study, contains hydrogen peroxide as part of its formulation; however, L* was no improved; Himonides et al (1999) used hydrogen peroxide as a bleacher in cod mince and found no significant differences for "L" values. Chow et al (2009), concluded that the increase in L* could be caused by the alkaline pH of the cryoprotectant used. However, as described previously our results showed an increment in L* value due to the washing treatment.…”

Section: Physicochemicalmentioning

confidence: 99%

Mince from Tilapia-Backbone: Effects of Washing and Cryoprotectant Addition during Frozen Storage

Lizárraga-Mata¹,

García-Sifuentes²,

Scheuren‐Acevedo³

et al. 2016

JFR

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Mince obtained from tilapia (Oreochromis niloticus) (backbone) was evaluated; the effect of washing and the addition of a commercial cryoprotectant on the quality of the mince obtained were also assessed. Physicochemical, microbiological and sensorial analyses were carried out at 0, 15, 30, 45, 60, 90, 120 and 180 days of frozen storage (-20 º C). During washing treatment 91% of lipids was removed from the mince (p<0.05). The proximal composition was stable during the storage time (p>0.05). Parameters such as L* and "θ" increased while a*, b*, chroma and TBARS decreased due to the washing treatment (p<0.05). The cryoprotectant effect resulted in a decrease of L*, "θ" (Hue) and TBARS (p<0.05). The addition of the cryoprotectant caused a significant decrease of L*, "θ" and TBARS. During the storage period, the proximate composition was stable and the microbial load remained below the official limits. The panelists detected changes on the odor, color and texture in the mince evaluated. Results suggest that the washing treatment improved the stability of the mince compared to the addition of cryoprotectant.

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Section: Physicochemicalmentioning

confidence: 99%

Mince from Tilapia-Backbone: Effects of Washing and Cryoprotectant Addition during Frozen Storage

Lizárraga-Mata¹,

García-Sifuentes²,

Scheuren‐Acevedo³

et al. 2016

JFR

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“…Mioglobin adalah protein globular yang mempunyai berat molekul berukuran kecil 17.000 kDa yang ditemukan pada daging (Chow et al 2009). Daging merah/gelap pada ikan tuna merupakan faktor penting dalam penentuan kualitas daging dan mempengaruhi faktor pembelian oleh konsumen.…”

Section: Pendahuluanunclassified

“…Analisis Mioglobin (Chow et al 2009) Sampel diblender hingga homogen, kemudian ditimbang sebanyak 1 g dalam tabung sentrifuse 50 mL dan ditambahkan 7 mL Aquabidest dingin, selanjutnya disentrifuse pada kecepatan 3000 G selama 15 menit. Sampel disaring dengan menggunakan kertas saring 0,2 µm.Sampel dipipet 1 mL, kemudian ditambahkan 0,5 mL pottasium buffer (25 µm pH 7) divortex, ditambahkan 25 µl larutan Na No 35%, divortex dan selanjutnya tambahkan 25 µl KCN 1%, divortex dan didiamkan selama 1 menit.…”

Section: Penyimpanan Bahan Bakuunclassified

Changesin Myoglobin of Big Eye Tuna During Chilling Storage

2015

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AbstrakTuna mata besar (Thunnus obesus) merupakan salah satu spesies ikan yang mempunyai potensi dalam meningkatkan sumber protein hewani, memiliki nilai ekonomis serta merupakan komoditas ekspor. Kesalahan penanganan dan penyalahgunaansuhutinggi dalam menangani tuna di daerah tropis dan sub tropis secara signifikan menurunkan nilai mioglobindan mempengaruhi kelarutan protein. Mioglobin adalah protein globular yang mempunyai berat molekul berukuran kecil yang merupakan faktor penting dalam penentuan kualitas daging dan mempengaruhi faktor pembelian oleh konsumen.Tujuan penelitian ini adalah menentukan perubahan kandungan mioglobin dan protein larut air beberapa bagian tuna mata besar (Thunnus obesus) selama sembilan hari pada suhu chilling. Bagian daging tuna mata besar yaitu perut, punggung dan ekor diambil dan dianalisis kandungan mioglobinnya baik daging terang maupun daging gelap. Kandungan mioglobin daging terang hari ke-0 daging bagian perut 121,68 mg/100g, bagian punggung 148,20 mg/100g, dan bagian ekor 105,16 mg/100g, setelah penyimpanan hari ke-9 mengalami penurunan menjadi 41,35 mg/100g untuk daging bagian perut, 52,01 mg/100g daging bagian punggung dan 31,34 mg/100g daging bagian ekor. Sedangkan pada daging gelap penyimpanan hari ke-0 bagian perut sebesar 418,64mg/100g, bagian punggung 446,21 mg/100g, bagian ekor 145,65 mg/100g, setelah hari ke-9 mengalami penurunan menjadi 121,01mg/100g untuk daging bagian perut, 58,34 mg/100g daging bagian punggung, dan 87,98 mg/100g daging bagian ekor. Protein larut air diperoleh pita-pita protein dengan berat molekul 15,4 kDa dan 14 kDa yang diduga sebagai protein mioglobin. Adanya perbedaan berat molekul diakibatkan telah terjadi perubahan atau degradasi protein selama proses penyimpanan.Kata kunci: Tuna mata besar, daging, penyimpanan, mioglobin Abstract Big eye tuna (Thunnus obesus) is one of the species of tuna which is have some value added such as have potential to improve animal protein sources, have high economic values as well as an export commodity. Mishandling and misapplication of high temparatures on the tuna handling at the tropics and sub tropics climate was significantly decreasing the value of myoglobin and affecting the solubility of protein. Myoglobin is a globular protein that have small molecular weight size and it was an important factor for determining the quality of meat and influencing factors of purchasing power by the consumer. The purpose of this experiments is to determining the changes of myoglobin content and the water soluble proteins content at some parts of big eye tuna in 9 days chilling temperatures. The portion which is analized was the ventral area, dorsal area and tail area. Myoglobin content in all portion above, both light and dark meat was analized. The results shows the decreased value of myoglobin content from first handling (day zero) until day ninth (days 9th) experiment. Each myoglobin contentfrom white meat at at ventral, dorsal and tail meat was decreased from 121.68 mg/100 into 41.35 mg/100, 148.2 mg/100g into 52.0...

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“…The water-soluble fraction (prepared as described above) was used for the measurement of Mb extractability, as a parameter for the extent of Mb insolubilization (Chen and Chow 2001;Chow et al, 2009). To 1 mL of the extract was added 0.5 mL of 25 mM potassium buffer (pH 7.0) and gently mixed.…”

Section: Measurement Of Mb Extractabilitymentioning

confidence: 99%

“…Many attempts have been made to investigate the quality of fish and meat (Chow et al, 1985(Chow et al, , 2009Trout, 1989;Chen and Chow, 2001;Duran et al, 2008;Faustman, 2010; Determination of Mb derivatives The following procedures were carried out at 0 − 4℃ unless otherwise stated. The meat slice samples were homogenized with 7 volumes of ice cold water under moderate speed for 1 min using a homogenizer (Polytron model PT 10 − 35, Kinematica AG, Littau, Switzerland).…”

Section: Introductionmentioning

confidence: 99%

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

Nurilmala

Ushio

Kaneko

et al. 2013

FSTR

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Four quality grades (excellent, good, acceptable, and "not acceptable") of yellowfin tuna meat (Thunnus albacares), as judged by a professional appraiser, were compared based on the red/ox state and extractability of myoglobin (Mb). As a result, the metMb ratio of the "not acceptable" grade of meat was significantly higher than that of the other higher-grade samples. In contrast, the highest ratio of oxyMb was found in the "excellent" meat, followed by good > acceptable > "not acceptable" meats. Color measurement revealed significant differences in a* value between the different grades of meat, but showed essentially no difference in L* and b* values. Both a* value and redness index (a*/b*) showed high correlation coefficients with metMb ratio. Mb extractability tended to be higher in the higher grade of meat. In conclusion, the commercial appraisal of tuna meat quality was demonstrated to be reliable. Keywords: tuna, meat, quality, color, myoglobin *To whom correspondence should be addressed. E-mail: aochiai@tokai-u.jp IntroductionSeven species of tunas are consumed around the world. Yellowfin tuna (Thunnus albacores), whose meat is characterized by a light red color and less fat, is one of the most commercially important and favored tuna species. This scombridae species inhabits tropical and subtropical waters around the world. Therefore, this species is generally exported to Japan from tropical countries, such as Indonesia, Taiwan, and so on (MMAF, 2012). A quality check is frequently performed before processing and transportation. Sensory analyses performed by experienced appraisers are generally carried out to determine freshness as a composite of qualitative traits. Color is one of the most important factors affecting consumer preferences. The meat color of tuna is closely related with myoglobin (Mb) content and the red/ox state of the heme iron.Mb is a small globular protein whose biological function is basically to temporarily store oxygen in skeletal and cardiac muscles for facilitation of respiration (Livingston et al., 1983), though new functions of Mb have been recently reported, such as nitrogen oxide scavenging activity (Cossins and Berenbrink, 2008;Flögel et al., 2010;Helbo et al., 2012). Generally, Mb content changes dependent on animal species, muscle part, age, and diet of the animal. Pale colored meat, such as chicken and pork, generally contain lower concentrations of Mb compared with red colored meat such as beef. Oxidative muscles, namely, slow skeletal muscle (including the dark muscle of fish) and heart muscle, contain abundant Mb. In scombridae fish such as tuna, abundant Mb is also found in fast skeletal muscle (also referred to as ordinary muscle, light muscle or white muscle).An iron atom of heme is placed in the hydrophobic region of Mb, binding the imidazole group of proximal histidine directly and distal histidine through a coordinate bond (Phillips and Schoenboen, 1981). The binding of oxygen, as well as the state of an iron atom in the heme pocket, contributes to the meat colo...

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Effects of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage

Cited by 23 publications

References 47 publications

Mince from Tilapia-Backbone: Effects of Washing and Cryoprotectant Addition during Frozen Storage

Mince from Tilapia-Backbone: Effects of Washing and Cryoprotectant Addition during Frozen Storage

Changesin Myoglobin of Big Eye Tuna During Chilling Storage

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

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