Mackerel Cathepsins B and L Effects on Thermal Degradation of Surimi

Jiang, Shann‐Tzong; Lee, Bai-Lin; Tsao, Ching-Yu; Lee, Jai-Jaan

doi:10.1111/j.1365-2621.1997.tb03991.x

Cited by 43 publications

(52 citation statements)

References 41 publications

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“…Proteolytic activity in muscles is high at temperatures above 508C and causes the rapid and severe degradation of myofibrillar proteins, particularly myosin (Wasson, Babbitt, & French, 1993). The results of the present study were similar to the work of Jiang, Lee, Tsao, & Lee (1997), who showed that cathepsins B and L or purified cathepsin B of mackerel muscle not only degraded MHC but also partially degraded actin in pH 6.5 or 7.0 after 5 h of incubation at 558C. Jiang et al (1996) indicated that actomyosin of mackerel surimi was incubated at 378C for 12 h; degradation of MHC at pH 6.0-7.5 might be due to the action of calpains.…”

Section: Degradation Of Bmpsupporting

confidence: 89%

Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer

Wang

Peng

Teng

et al. 2013

CyTA - Journal of Food

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Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer, CyTA -Journal of Food, 11:1, 50-59, DOI: 10.1080/19476337.2012 To link to this article: https://doi.org/10. 1080/19476337.2012.684357 Copyright Taylor and Francis Group, LLC The activity of crude extracts from Alaska Pollock muscle responsible for the hydrolysis of myofibrils and perimysia from beef Longissimus Dorsi muscle was investigated. The results showed that myosin heavy chain and myosin light chain were hydrolyzed completely after 12 h of incubation. Tropomyosin, a-actinin, and troponin-T disappeared after 24 h of incubation, whereas the actin was partially degraded. The collagen fibers were so loose that cross-linking among microfibrils occurred after treatment with the crude extracts. Meanwhile, the second structures of myofibrillar proteins were not changed markedly after incubation. The ahelices in perimysia treated with the crude extracts were partially transformed into b-sheets, while the b-turn and the random coil fractions were steady. It was concluded that myofibrils and perimysia from beef Longissimus Dorsi muscle were commendably hydrolyzed by the crude extracts from Alaska Pollock muscle, so that the crude extracts from Alaska Pollock muscle could be utilized as a potential meat tenderizer.Keywords: beef; Alaska Pollock; crude extracts; incubation; myofibrillar proteins; perimysia Se investigo´la actividad de extractos no purificados de mu´sculo de abadejo Alaska responsables de la hidro´lisis de miofibrilos y perimisios de mu´sculo Longissimus Dorsi de buey. Los resultados mostraron que las miosinas de cadena pesada (MHC) y las miosinas de cadena liviana (MLC) fueron hidrolizadas completamente tras 12 h de incubacio´n. La tropomiosina, actinina ay troponina T desaparecieron tras 24 h de incubacio´n, mientras la actina fue parcialmente degradada. Las fibras cola´genas estaban tan sueltas que el entrecruzado entre microfibrilos tuvo lugar tras el tratamiento con los extractos no purificados. Mientras, las segundas estructuras de proteı´nas miofibrilares no mostraron un cambio marcado tras la incubacio´n. Las he´lices a en perimisios tratados con extractos no purificados fueron parcialmente transformados en la´minas beta, mientras las fracciones de giro beta y de espiral aleatoria se mostraron constantes. Se concluyo´que puesto que miofibrilos y perimisios procedentes de mu´sculo Longissimus Dorsi de buey fueron remarcablemente hidrolizables con extractos no purificados de mu´sculo de abadejo Alaska, estos extractos podrı´an ser utilizados como potencial ablandador de carne.

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Section: Degradation Of Bmpsupporting

confidence: 89%

Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer

Wang

Peng

Teng

et al. 2013

CyTA - Journal of Food

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show abstract

“…However, when stored for a longer time, the activities changed little. Jiang et al (1997) found that 82% of activities of purified cathepsin in mackerel remained even after 8 weeks when stored at pH 6.5, at À40°C. In our research, cathepsins were also found to be relatively stable for a week at low temperature (4°C) in acidic environment, especially cathepsin L.…”

Section: Proteolytic Activities During Fermentation and Storagementioning

confidence: 98%

“…This is in accordance with our results, showing a decline in collagenolytic activity and an increase in catheptic activities during fermentation. The activation of cathepsins by the decline in pH may be due to conversion from precursor or intermediate forms into mature form by acidification and leakage of lysosomal enzymes caused by rupture of membranes (Jiang, Lee, Tsao, & Lee, 1997;Liu, Yin, Zhang, Li, & Ma, 2006. The inactivation of collagenase was due to its instability under acidic conditions (Simpson, 2000).…”

Section: Proteolytic Activities During Fermentation and Storagementioning

confidence: 98%

Endogenous proteolytic enzymes – A study of their impact on cod (Gadus morhua) muscle proteins and textural properties in a fermented product

Yang

Rustad

et al. 2015

Food Chemistry

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“…Estudos feitos por Jiang et al (1997) com peixes (Scomber australasicus) preparados para surimi demonstram que as catepsinas B e L conservam 82% da sua atividade enzimática após congelamento, por oito semanas, a -40ºC. Pode-se, então, supor que, a conservação das proteínas miofibrilares das amostras é devida à liofilização e não ao congelamento.…”

Section: Eletroforese Em Sds-pageunclassified

Preparo e caracterização de proteínas miofibrilares de tilápia-do-nilo para elaboração de biofilmes

Monterrey-Quintero

Sobral

2000

Pesq. agropec. bras.

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EDNELÍ SORAYA MONTERREY-QUINTERO2 e PAULO JOSÉ DO AMARAL SOBRAL 3 RESUMO -A elaboração de filmes comestíveis à base de biopolímeros implica conhecimento das propriedades físico-químicas da macromolécula. Os objetivos deste trabalho foram a descrição de um método de preparo de proteínas miofibrilares de tilápia-do-nilo (Oreochromis niloticus), o estudo das propriedades relacionadas com a formação de filmes, e a caracterização dos biofilmes elaborados com a proteína. Músculo moído de tilápia-do-nilo, recém-abatida, foi lavado e processado até formação de uma pasta homogênea. A evolução das frações protéicas, durante o processamento, foi acompanhada por calorimetria diferencial de varredura. Estudou-se a solubilidade das proteínas miofibrilares liofilizadas (PML) em função do pH (2-7). A identificação das frações protéicas e dos aminoácidos foi realizada por SDS-PAGE e cromatografia de troca iônica, respectivamente. Os biofilmes formados foram submetidos a testes de perfuração, de solubilidade e microscopia eletrônica. A amostra de PML, constituída apenas de proteínas miofibrilares, apresentou uma região de máxima solubilidade (96,9%) em torno do pH 3,0 e elevado potencial de interações iônicas (74,4 kJ/100 kJ). Os biofilmes à base das PML de tilápia-do-nilo são pouco solúveis (abaixo de 20 g/100 g matéria seca). O glicerol influencia fortemente as propriedades mecânicas e a solubilidade dos biofilmes.Termos para indexação: filmes comestíveis, propriedades funcionais, propriedades mecânicas, solubilidade. EXTRACTION AND PROPERTIES OF NILE TILAPIA MYOFIBRILLAR PROTEINS FOR EDIBLE FILMSABSTRACT -The elaboration of edible films based on biopolymers, implies the knowledge of physicochemical properties of macromolecules. The objectives of this work were to describe a methodology of preparing Nile Tilapia myofibrillar proteins and study the properties related to formation and characterization of edible film elaborated with these proteins. Freshly slaughtered ground Nile Tilapia (Oreochromis niloticus) muscle was washed and processed until the formation of a homogeneous paste. Evolution of protein fractions during processing was followed by scanning differential calorimetry. Solubility of freeze-dried myofibrillar proteins was studied as a function of pH (2-7). Identification of protein fractions and that of the composition of amino acids were accomplished by SDS-PAGE and ion-exchange chromatography, respectively. Biofilms, thus formed, were submitted to puncture, solubility and scanning electron microscopy tests. The sample of freeze-fried proteins, constituted only of myofibrillar proteins, presented maximum solubility (96.9%), at pH around 3 and a high ionic interaction potential (74.4 kJ/100 kJ). Nile Tilapia myofibrillar protein based biofilms were not very soluble (lower than 20 g/100 g dry matter). Glycerol strongly influenced mechanical as well as solubility properties of biofilms.

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Mackerel Cathepsins B and L Effects on Thermal Degradation of Surimi

Cited by 43 publications

References 41 publications

Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer

Potential use of crude extracts from Alaska Pollock muscle as meat tenderizer

Endogenous proteolytic enzymes – A study of their impact on cod (Gadus morhua) muscle proteins and textural properties in a fermented product

Preparo e caracterização de proteínas miofibrilares de tilápia-do-nilo para elaboração de biofilmes

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