Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Park, Pyo Jam; Lee, Sang Hoon; Byun, Hee Guk; Kim, Seo Hyun; Kim, Se‐Kwon

doi:10.5483/bmbrep.2002.35.6.576

Cited by 31 publications

(42 citation statements)

References 22 publications

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“…The optimum temperature depends on the type of enzyme, the analyzed tissue and the source species, and has been reported for collagenolytic enzymes in the range of 30°C and 60°C PARK et al, 2002;DABOOR et al, 2012;WU et al, 2010a;HAYET et al, 2011;SUPHATHARAPRATEEP et al, 2011;BAEHAKI et al, 2012;LIMA et al, 2013). Similar results to the present study were described for winter flounder P. americanus (TERUEL and SIMPSON 1995), filefish species N. modestrus , tuna T.…”

Section: Temperature and Ph Assay Of The Collagenolytic Enzymesupporting

confidence: 81%

“…Hydrolysis of type I collagen has been detected by using collagenolytic proteases produced by various aquatic organisms, such as for the species of fish described by: KRISTJÁMSSON et al (1995) for Atlantic cod (G. morhua); TERUEL and SIMPSON, (1995) for winter flounder (P. americanus); BYUN et al (2002) for tuna (T. thymus); PARK et al (2002) for mackerel (S. japonicus); KIM et al (2002) for filefish (N. modestrus); HERREIRO-HERNANDEZ et al (2002) for iced cod (G. morhua); HAYET et al (2011) for sardinelle (S. aurita);and ROY et al (1996) for greenshore crab (C. maenas). In our studies, the intestinal protease of smooth weakfish was able to cleave the collagen type I tested, as shown in Figure 3.…”

Section: Hydrolysis Of Collagen By the Collagenolytic Enzymementioning

confidence: 99%

“…The measure of the digestion of native collagen type I was performed according to the method of MOORE andSTEIN (1954) andPARK et al, (2002) with a slight modification. A reaction mixture, which contained 5 mg of collagen, 1 mL of 50 mM Tris-HCl (pH 7.5 with 5 mM CaCl2) and 0.1 mL of the enzyme solution, was incubated at 37°C for 12, 24, 36 and 48 hours.…”

Section: Hydrolytic Capacity Assay With Collagenmentioning

confidence: 99%

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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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Section: Temperature and Ph Assay Of The Collagenolytic Enzymesupporting

confidence: 81%

Section: Hydrolysis Of Collagen By the Collagenolytic Enzymementioning

confidence: 99%

Section: Hydrolytic Capacity Assay With Collagenmentioning

confidence: 99%

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

et al. 2017

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“…Teruel and Simpson (1995) isolated a collagenolytic enzyme from the skeletal muscle of winter flounder with greatest activity at a pH of 7.5 while the most enzyme activity of collagenolytic serine proteases isolated from digestive tracts of various fish and aquatic invertebrates (including crabs, prawns, crayfish and cod) is within the pH range of 6.5-8.0 . Other studies found slightly higher pH values (7.0-8.0) to be optimal for collagenolytic activity in the digestive tissues of crabs, mackerel and file fish (Sivakumar, et al, 1999;Park et al, 2002). Extremes of pH are to be avoided.…”

Section: Factors Affecting Collagenase Activitymentioning

confidence: 99%

“…Thus, particular care should be taken when using this method on semipurified extracts, with particular emphasis placed on blank measurements (Lim et al, 1993). Despite this limitation, this assay remains a relatively simple method to perform and a number of studies have successfully used it with minor modifications of the incubation time and/or the amount of the substrate to determine collagenases isolated from a variety of sources (Rosen, 1957;Yoshida and Noda, 1965;Endo et al, 1987;Sivakumar et al, 1999;Yin et al, 2002;Park et al, 2002;Wu et al, 2010). …”

Section: Colorimetric Assaysmentioning

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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Collagenase produced from Aspergillus sp. (UCP 1276) using chicken feather industrial residue

Ferreira

Correia

Costa

et al. 2016

Biomedical Chromatography

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An extracellular collagenolytic serine protease was purified from Aspergillus sp., isolated from the Caatinga biome in northeast Brazil by a two-step chromatographic procedure, using an anion-exchanger and gel filtration. The enzyme was produced by submerged fermentation of feather residue as a substrate. The purified collagenase showed a 2.09-fold increase in specific activity and 22.85% yield. The enzyme was a monomeric protein with a molecular mass of 28.7 kDa, estimated by an SDS-PAGE and AKTA system. The optimum temperature and pH for enzyme activity were around 40°C and pH 8.0, respectively. The enzyme was strongly inhibited by phenyl-methylsulfonyl fluoride, a serine protease inhibitor, and was thermostable until 65°C for 1 h. We then evaluated the enzyme's potential for degradation of Type I and Type V collagens for producing peptides with antifungal activity. Our results revealed that the cleavage of Type V collagen yielded more effective peptides than Type I, inhibiting growth of Aspergillus terreus, Aspergillus japonicus and Aspergillus parasiticus. Both groups of peptides (Type I and Type V) were identified by SDS-PAGE. To conclude, the thermostable collagenase we purified in this study has various potentially useful applications in the fields of biochemistry, biotechnology and biomedical sciences.

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Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus

Cited by 31 publications

References 22 publications

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

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

Collagenase produced from Aspergillus sp. (UCP 1276) using chicken feather industrial residue

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