Biochemical Effects of High Hydrostatic Pressure on the Lysosome and Proteases Involved in It

Ohmori, Takashi; Shigehisa, Tamotsu; Taji, Siro; Hayashi, Rikimaru

doi:10.1271/bbb.56.1285

Cited by 53 publications

(34 citation statements)

References 9 publications

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“…Calpains are active at early stages, while the action of cathepsin B is related to the degree of post-mortem lysosomal membrane breakdown, which occurs due to permeabilisation of the lysosomal membrane related to depletion of ATP reserves and malfunctioning of ionic pumps (Sentandreu et al, 2002). Ohmori et al (1992) indicated that application of high pressures to fresh meat induces release of cathepsins from lysosomes, producing an enhancement of proteolytic activity. The magnitude of this increase is the balance of two contrasting phenomena: the release of cathepsins from the lysosomes and the inactivation of the enzymes by pressure.…”

Section: Sds-page and Immunoblottingmentioning

confidence: 99%

Stress relaxation behaviour and structural changes of muscle tissues from Gilthead Sea Bream (Sparus aurata L.) following high pressure treatment

Campus

Addis

Cappuccinelli

et al. 2010

Journal of Food Engineering

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Section: Sds-page and Immunoblottingmentioning

confidence: 99%

Stress relaxation behaviour and structural changes of muscle tissues from Gilthead Sea Bream (Sparus aurata L.) following high pressure treatment

Campus

Addis

Cappuccinelli

et al. 2010

Journal of Food Engineering

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“…However, HPP can affect also proteins, particularly myofibrillar proteins, which results in structural modifications and texture changes in muscle foods (Angsupanich et al 1999). In addition, HPP can disrupt lysosomal membranes causing the release into the fish muscle of enzymes, such as cathepsins, leading to possible alterations of myofibrillar proteins mediated by these enzymes (Ohmori et al 1992).…”

mentioning

confidence: 99%

High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle

Fidalgo¹,

Saraiva

Aubourg³

et al. 2014

Czech J. Food Sci.

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We determined high pressure processing (HPP) effects on the activities of cathepsins B and D in the muscles of mackerel (Scomber scombrus) and horse mackerel (Trachurus trachurus). In mackerel, the cathepsin B activity decrease reached 40% at 450 MPa while in horse mackerel, low and intermediate pressures (150 and 300 MPa) caused an activity increase (30%) but at 450 MPa a decrease of up to 60%. In both species, cathepsin D activity increased after a 300 MPa treatment (up to 2-fold for mackerel and 60% for horse mackerel) and decreased on a 450 MPa treatment. The activity increase is probably due to HPP damage of lysosome releasing enzymes into the fish muscle. Based on the HPP effects on the activities of cathepsins B and D, 450 MPa may be used to reduce the proteolytic activity of cathepsin B prior to chilled or frozen storage of these fish species.Keywords: high pressure processing; fish; Scomber scombrus; Trachurus trachurus; mackerel and horse mackere; proteolytic enzymesSmall pelagic fish species, such as the Atlantic mackerel (Scomber scombrus) and Atlantic horse mackerel (Trachurus trachurus), are important fishery resources in many coastal areas of South European countries (Mbarki et al. 2009). Horse mackerel has been attracting great attention because of its moderate price and large quantities captured in West-European countries

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“…The application of 30-and 10-kDa membranes increased recovery effectiveness to 114-119 and 79-124% compared to crude brine, respectively (Table 1). High pressure, likewise ultrasound or freezing, induces damage to membranes of lysosomes and release of enzymes, without causing damage to cathepsins (Ohmori et al, 1992;Jang et al, 2000;Karshafian, 2010;Toldra & Reig, 2015). The losses of cathepsins D + E activity to 30-and 10-kDa permeates were lower than the losses of cathepsins B + L (Table 1); however, the activity of cathepsin E was noted only in the 100-kDa permeate (data not shown).…”

Section: Nanofiltrationmentioning

confidence: 89%

Recovery of cathepsins from marinating brine waste

Szymczak

2016

Int J of Food Sci Tech

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Summary In the fish industry, brine left after herring marinating is discarded to waste. This study presents laboratory‐scale findings regarding recovery of aspartyl (D + E) and cysteine cathepsins (B + L) from waste brine. Ultrafiltration enabled cathepsin recovery from both the soluble and lysosomal fraction of the marinating brine. Retentate 10 kDa had the highest cathepsin activity 140% compared to crude brine. The amount of recovered cathepsins using membranes 30 and 100 kDa was less than 10 kDa, because part of cathepsins passes to permeate. In turn, the salting‐out with ammonium sulphate enabled activity recovery of only 80%, but ensured over twofold higher purity of the enzymes than ultrafiltration. The highest precipitation of D + E cathepsins was noted at salt concentration of 40–60%, whereas that of B + L cathepsins at 50–80%. It is recommended to dissolve the salted‐out aspartyl cathepsins at pH 4.0 or 8.0, whereas the cysteine ones at pH 5.0. The appropriate selection of parameters enables controlling the aspartyl to cysteine cathepsins ratio in the preparation in the range from 1:2 to 2:1. The new cathepsin preparations showed high activity in a wide range of pH values and ionic strength and can be used in food production.

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Biochemical Effects of High Hydrostatic Pressure on the Lysosome and Proteases Involved in It

Cited by 53 publications

References 9 publications

Stress relaxation behaviour and structural changes of muscle tissues from Gilthead Sea Bream (Sparus aurata L.) following high pressure treatment

Stress relaxation behaviour and structural changes of muscle tissues from Gilthead Sea Bream (Sparus aurata L.) following high pressure treatment

High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle

Recovery of cathepsins from marinating brine waste

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