Purification and characterization of a novel cysteine proteinase from mackerel (Scomber australasicus)

Jiang, Shann‐Tzong; Lee, Jai-Jaan; Chen, Hsing-Chen

doi:10.1021/jf00044a011

Cited by 14 publications

(10 citation statements)

References 29 publications

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“…In our endeavors through a series of investigations of the participation of muscle cysteine proteinases in postmortem tenderness of fish muscle, cathepsins L and L-like (Lee et al, 1993) and B (Jiang et al, 1994a) and a novel cysteine proteinase (designated cathepsin X; Jiang et al, 1994b) have been purified from mackerel. This study was undertaken to compare the degradation profiles of myofibrillar proteins produced by these proteinases.…”

Section: Introductionmentioning

confidence: 99%

Proteolysis of Actomyosin by Cathepsins B, L, L-like, and X from Mackerel (Scomber australasicus)

Jiang

Lee

Chen

1996

J. Agric. Food Chem.

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Cathepsins B and L and cathepsin L-like proteinase degraded myosin heavy chain of actomyosin (AM) into several fragments with molecular masses (MW) of 154, 146, 138, 67, and 36 kDa; 164 and 155 kDa; and 135, 128, and 69 kDa, respectively. In the presence of 0.6 M NaCl, however, the MHC was degraded by cathepsin L into 164, 155, 41, and 37 kDa fragments. The hydrolytic rate of these three proteinases on AM was faster at pH 5.0 than at pH 6.0. Actin seemed to be resistant against hydrolysis by cathepsins B, L, and L-like in the absence of 0.6 M NaCl. According to SDS−PAGE analysis, cathepsin X, a novel cysteine proteinase, did not degrade AM. Keywords: Mackerel; cathepsins; actomyosin; proteolysis; seafood

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Section: Introductionmentioning

confidence: 99%

Proteolysis of Actomyosin by Cathepsins B, L, L-like, and X from Mackerel (Scomber australasicus)

Jiang

Lee

Chen

1996

J. Agric. Food Chem.

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“…Studies on unparasitized Japanese flounder have shown a cathepsin L-like protease as the cause of softening (Toyohara et al 1993b). Several cysteine proteases have been isolated from nonparasitized mackerel Scomber australasicus including cathepsin B (Jiang et al 1994a), cathepsin L and another cathepsin L-like protease (Lee et al 1993) as well as a higher molecular weight cysteine protease (Jiang et al 1994b).…”

Section: Introductionmentioning

confidence: 99%

Comparison of Cathepsin B, D, H and L Activity in Four Species of Pacific Fish

Porter

Koury

Stone

1995

J Food Biochemistry

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The activities of cathepsins B, D, H and L were compared in crude muscle extracts from four species of fish: Pacific whiting (PW), (Merluccius productus); arrowtooth flounder (ATF), (Atheresthes stomias); Alaska pollock (AP), (Theragra chalcogramma); and Pacific cod (PC), (Gadus macrocephalus). Both PW and ATF are known to undergo softening during post‐mortem handling and cooking while AP and PC do not. Cathepsin B and L activities were both higher in extracts of PW and ATF than in AP and PC. Cathepsins B and L activities were both much higher in PW than in ATF. Cathepsin H activity was highest in AP followed by ATF with PC and PW having the lowest activities. Cathepsin D activity was extremely low in all four species. The heat stability of the various cathepsin activities showed cathepsin B to be the most heat labile and was inactivated by 50C heating for 15 min. Cathepsin H activity was inactivated at 60C, while cathepsin L required 70C for inactivation. Cathepsins B and L are the most likely responsible for softening in PW and ATF during holding and subsequent processing. However, during cooking, cathepsin L likely causes the most damage since it requires 70C for inactivation. The difference in heat stability of cathepsins B and L can be used to differentiate between their activities.

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“…The activation energy ( E a ) of inactivation was obtained from the slope of the Arrhenius plots of Ln k against the reciprocal of incubation temperature (1/T). Thermodynamic functions were calculated according to Eyring transition state theory, as described by Jiang et al . (1994), used for irreversible heat inactivation of cysteine protease as follows:…”

Section: Methodsmentioning

confidence: 99%

Analysis of Thermal Inactivation Kinetics of Membrane-Bound Polyphenol Oxidases and Peroxidases From Metroxylon Sagu

Onsa¹,

Hamid²,

Selamat³

et al. 2011

Journal of Food Biochemistry

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Thermal inactivation kinetics for the purified membrane‐bound polyphenol oxidases (mPPOs) and peroxidases (mPODs) isolated from Metroxylon sagu were analyzed. Each isoenzyme was treated at different time–temperature combinations in the range of 0–70 min and 20–70C. Thermal inactivation rates constant (k) at 70C for mPOD‐I (72.9 × 10‐3/min) and mPOD‐II (97.9 × 10‐3/min) were lower than that of mPPO‐I (379.7 × 10‐3/min) and mPPO‐II (138.1 × 10‐3/min). The activation energy for inactivation of mPPO‐I (32.94 kcal/mol) and mPPO‐II (40.34 kcal/mol) was lower compared with mPOD‐I (45.77 kcal/mol) and mPOD‐II (40.62 kcal/mol). The enthalpy values for mPOD‐I (45.08 kcal/mol) and mPOD‐II (39.94 kcal/mol) were higher than those of mPPOs (mPPO‐I, 32.26 kcal/mol; mPPO‐II, 39.66 kcal/mol). This result implies that both mPOD‐I and mPOD‐II are more thermostable. PRACTICAL APPLICATIONS Sago starch has a great potential for application in various food systems. However, its further development and exploitation was hindered by browning‐associated problems due to polyphenol oxidases and peroxidases. In this work, we have investigated the effect of heat treatment on the stability and inactivation kinetics of membrane‐bound polyphenol oxidases and membrane‐bound peroxidases. The results from this work will enable the food industry to develop optimum process parameters with respect to heating time and temperature during processing and production of sago starch to produce high‐quality starch.

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Purification and characterization of a novel cysteine proteinase from mackerel (Scomber australasicus)

Cited by 14 publications

References 29 publications

Proteolysis of Actomyosin by Cathepsins B, L, L-like, and X from Mackerel (Scomber australasicus)

Proteolysis of Actomyosin by Cathepsins B, L, L-like, and X from Mackerel (Scomber australasicus)

Comparison of Cathepsin B, D, H and L Activity in Four Species of Pacific Fish

Analysis of Thermal Inactivation Kinetics of Membrane-Bound Polyphenol Oxidases and Peroxidases From Metroxylon Sagu

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