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

Sovik, Siri Lise; Rustad, Turid

doi:10.1016/j.lwt.2004.11.006

Cited by 20 publications

(7 citation statements)

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“…According to Kristjánsson et al (1995), the collagenolytic enzyme in Atlantic cod was stable in the pH range between approximately 7.0-9.5 when incubated at 25°C for 30 min, but a sharp decrease in the stability of the enzyme occurred at pH values below 7. Although Sovik and Rustad (2006) showed that the collagenase had high heat stability at 30°C, long time exposure in acidic environment led to quick loss of collagenolytic activity in our study.…”

Section: Proteolytic Activities During Fermentation and Storagecontrasting

confidence: 57%

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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Section: Proteolytic Activities During Fermentation and Storagecontrasting

confidence: 57%

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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“…DABOOR et al (2012) found an optimal activity of 35°C using a mixture of haddock, herring, ground fish and flounder; and at the same time a temperature of 30°C was reported by ROY et al (1996) when studied greenshore crab (Carcinus maenas). SOVIK and RUSTAD (2006) verified a decrease in the enzyme activity in temperatures below 35°C in the guts of prey Brosme brosme and Molva molva, while MUKHERJEE et al (2009), studying sponge (Rhopaloeides odorabile), observed an optimal enzyme activity at 30°C. Enzymes with collagenolytic properties from microbial sources are often objects of investigation, having been reported by WU et al (2010b) when they studied bacterial strains of Bacillus pumilus and determined an optimal enzyme activity at 45°C, showing that more than 50% of residual activity was lost after 5 min of incubation at 70°C or 10 min at 60°C.…”

Section: Temperature and Ph Assay Of The Collagenolytic Enzymementioning

confidence: 81%

Colagenase de pescada branca: extração, purificação parcial, caracterização e teste de especificidade ao colágeno para aplicação industrial

et al. 2017

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Fish processing residues are rich sources of biomolecules with industrial potential, such as enzymes with collagenolytic properties applied in the pharmaceutical, textile and leather sectors. Here, collagenolytic serine proteases were partially purified from the waste (viscera) of smooth weakfish Cynoscion leiarchus and characterized for the purpose of obtaining a value-added product from fisheries resources. The higher activity of the enzyme (72.5 U mL -1 ) was verified in optimal temperature and pH of 55°C and 8.0, respectively. The enzyme was stable in wide ranges of temperature (25-60°C) and pH (6.5 to 11.5). The ions Ca 2+ and Mg 2+ increased the protease activity, whilst Pb 2+, Al 3+ and Cu 2+ had an inhibitory effect, as observed in the presence of Benzamidine and TLCK (inhibitors of serine proteases). Hydrolysis was detected after 48 hours, when the enzyme and bovine collagen type I were incubated together. Thus, digestive viscera of C. leiarchus is suggested as an alternative source of enzymes capable of cleaving type I collagen, with similar biochemical properties to bacterial collagenases commonly employed in industrial processes, reducing costs, adding value to the fisheries product and minimizing the environmental impact caused by its waste. , com temperatura e pH ótimos de 55°C e 8.0, respectivamente. A enzima manteve-se estável em faixas amplas de temperatura (25-60 °C) e pH (6,(5)(6)(7)(8)(9)(10)(11)5 , Al 3+ e Cu 2+ inibiram essa atividade assim como os inibidores de serino-proteases (Benzamidina e TLCK). A hidrólise foi detectada após 48h de incubação com colágeno bovino tipo I. Assim, sugere-se vísceras digestivas de C. leiarchus como fonte alternativa para o fornecimento de enzimas com capacidade de clivar o colágeno do tipo I e com propriedades bioquímicas semelhantes às colagenases bacterianas já empregadas nas etapas de processamento industrial, como forma de redução de custo, agregação de valor ao produto pesqueiro e contribuindo para minimizar o impacto ambiental deste tipo de resíduo.

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“…Sovik and Rustad (2006) reported that a decrease in enzyme activity seems to become an issue at temperatures >35°C in viscera from tusk (Brosme brosme) and ling (Molva molva). Teruel and Simpson (1995) reported that tissues isolated from other fish such as muscle in winter flounder yielded collagenases that began to denature at temperatures >40°C.…”

Section: Factors Affecting Collagenase Activitymentioning

confidence: 99%

“…Several researchers (Eizen and John, 1969;Zefirova et al, 1996;Sivakumar et al, 1999) showed that the temperature for optimal activity is tissue and species specific. Sovik and Rustad (2006) showed that metallocollagenases isolated from the muscle of cod had maximum activity at 20°C, while maximum activity of serine collagenases isolated from the viscera of the same species was at 50°C. Despite this high degree of variation, it would seem that temperatures <20°C should be sufficient to preserve collagenolytic activity in most tissues.…”

Section: Factors Affecting Collagenase Activitymentioning

confidence: 99%

Extraction and Purification of Collagenase Enzymes: A Critical Review

Daboor¹,

Budge²,

Ghaly

et al. 2010

American Journal of Biochemistry and Biotechnology

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Problem statement: Enzymes have vital roles in several industrial processes (foods, cosmetics, nutraceuticals and pharmaceuticals) due to their highly selective nature and high activity at very low concentrations. Recent efforts to identify new sources of useful enzymes have been concentrated on the marine environment because of the potential to make use of processing wastes. About 35-50% of the mass of the fish caught is a waste that is disposed off at sea or in landfills. The extraction of enzymes from fish processing waste can reduce environment problems and improve the economics of the fish industry. Collagenases are a group of enzymes that can be extracted from fish waste. Approach: Comprehensive reviews of the literature on the extraction, purification, characterization and use of collagenases was carried out. Results: Collagenases have different molecular weights based on their types and sources. They have the ability to break down the peptide bonds in collagen at physiological pH. They are classified into two types: serine and metallocollagenase. Collagenolytic activities have been shown at a wide range of temperatures (20-40°C) and pH (6-8). Many activators can be used to achive collagenase activity including 4-Aminophenylmercuric Acetate (APMA), trypsin, potassium or sodium thiocyanate, iodoacetamide and potassium iodide. Dithiothreitol (DTT), mercaptoethanol, ethylendiaminetetracetic acid, ophenanthroline and cysteine inactivate the enzyme. Collagenases enzymes can be extracted with a variety of techniques using different buffering systems (tris-HCl, sodium bicarbonate, calcium chloride and cacodylate). All techniques involve the use of ammonium sulphate fractionation and centrifugation to precipitate the enzyme. Collagenases are normally purified using chromatographic techniques such as gel-filtration, ion-exchange and affinity column chromatography. Collagenase can be assayed with a number of methods, including: colorimetric absorbance, viscometry, radioactivity and fluorescence spectroscopy. Collagenases are partly responsible for toughness in red meats and are used as tenderizers in food industry, have application in the fur and hide tanning to ensure uniform dying of leather, used in medicine to treat burns and ulcers, eliminate scar tissues, transplantation of organs. Conclusion: Understanding of the nature of the enzymes and identifying the most suitable resources and the methods for their extraction and purification will have significant impact on the fish processing, food and medical industries.

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

Cited by 20 publications

References 50 publications

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

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

Colagenase de pescada branca: extração, purificação parcial, caracterização e teste de especificidade ao colágeno para aplicação industrial

Extraction and Purification of Collagenase Enzymes: A Critical Review

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