Purification and Characterization of Cathepsin B from Ordinary Muscle of Mackerel (Scomber australasicus)

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

doi:10.1021/jf00041a005

Cited by 44 publications

(38 citation statements)

References 42 publications

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“…Cathepsin B from hepatopancreas (a digestive gland) of carp (Cyprinus carpio) has been found to have a temperature maximum of 45 1C (pH 6) (Aranishi, Hara, Ossatomi, & Ishihara, 1997). Cathepsin B from mackerel (Scomber australasicus, Scomber japonicus) muscle showed temperature optimum at 55 1C (pH 6.5) (Jiang, Lee, & Chen, 1994;Jiang, Lee, Tsao, & Lee, 1997) and from Mujil auratus muscle at 45 1C (pH 6.0) (Bonete Manjon, Llorca, & Iborra, 1984b). In fillets of Pacific whiting (Merluccius productus), cathepsin B had maximum activity between 20 and 37 1C (An, Weerasinghe, Seymour, & Morrissey, 1994).…”

Section: Effect Of Speciesmentioning

confidence: 99%

Effect of season and fishing ground on the activity of cathepsin B and collagenase in by-products from cod species

Sovik

Rustad

2006

LWT - Food Science and Technology

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Section: Effect Of Speciesmentioning

confidence: 99%

Effect of season and fishing ground on the activity of cathepsin B and collagenase in by-products from cod species

Sovik

Rustad

2006

LWT - Food Science and Technology

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“…According to the properties of cathepsins B, L and L-like and the present results, these proteinases should be very important 50-MIP in mackerel surimi. 4,6,27,49,50 Nevertheless, the exact mechanism of protein-induced softening still needs to be clarified.…”

Section: Calpain Cathepsins L And/or L-like Effects On Gel Softeningmentioning

confidence: 99%

Effects of mackerel cathepsins L and L-like, and calpain on the degradation of mackerel surimi

Chen

Jiang

2000

Fisheries Sci

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SUMMARY : During surimi processing, the total cathepsins B+L+L‐like activities in minced, leached and NaCl‐ground meats were 2.45, 2.07 and 1.77 units/g, respectively. There was still 77% activity left even after 8 weeks storage at –20°C. High calpain and calpastatin activities in the crude enzymes from frozen mackerel surimi suggested that they were difficult to remove during processing and very stable during frozen storage. The SDS‐PAGE analysis indicated that the optimal conditions for the hydrolysis of myosin heavy chain (MHC) were 40–55°C, pH 5.5–7.0 for cathepsins L and L‐like and pH 7.0–7.5 for calpain. The gel strength of surimi treated with calpain did not decrease significantly, but the strength of those treated with purified cathepsins L and/or L‐like decreased significantly (P < 0.05) after 2 h incubation at 55°C. These results suggested that cathepsins L and L‐like left in surimi had MHC‐degrading ability which consequently caused gel softening during setting at 40–55°C.

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“…Cathepsins B (Jiang et al, 1994) and L from mackerel (Lee et al, 1993) have been purified. Both enzymes could degrade actomyosin into low molecular weight fragments (Jiang et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Mackerel Cathepsins B and L Effects on Thermal Degradation of Surimi

Jiang¹,

Lee²,

Tsao³

et al. 1997

Journal of Food Science

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During surimi processing, cathepsins B and L activities in minced, leached and NaCl-ground meats were 6.02, 5.23, and 4.07 units/g, respectively. About 80% activity remained in surimi after 8 wk storage at Ϫ40ЊC suggesting that these proteinases were stable and difficult to remove. At 40Њϳ55ЊC, pH 6.5ϳ7.5, cathepsins B and L and purified cathepsin B had high hydrolytic activity on myosin heavy chain (MHC). The strength of surimi gel with cathepsins B and L or with purified B decreased (pϽ0.05) after 2 hr incubation at 55ЊC. This suggested that the residual cathepsins B and L had MHC-degrading activity and consequently caused gel softening.

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Purification and Characterization of Cathepsin B from Ordinary Muscle of Mackerel (Scomber australasicus)

Cited by 44 publications

References 42 publications

Effect of season and fishing ground on the activity of cathepsin B and collagenase in by-products from cod species

Effect of season and fishing ground on the activity of cathepsin B and collagenase in by-products from cod species

Effects of mackerel cathepsins L and L-like, and calpain on the degradation of mackerel surimi

Mackerel Cathepsins B and L Effects on Thermal Degradation of Surimi

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