Collagenolytic Activity of Cured Hide Bacteria

Woods, David R.; Welton, R. L.; Thomson, Jennifer A.; Cooper, D.R.

doi:10.1111/j.1365-2672.1972.tb03681.x

Cited by 18 publications

(3 citation statements)

References 4 publications

(4 reference statements)

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“…Although several microbial elastases and collagenases, in addition to pancreatic elastase, have so far been isolated and characterized (Morihara and Tsuzuki, 1967; Woods et al, 1972; Shiio et al, 1974;Terato et al, 1976), these enzymes were not successful in meat products due to safety problems, such as pathogenicity, or other disadvantageous effects (Foegeding and Larick, 1986; Bernal and Stanley, 1987; Cronlund and Woychik, 1987;Miller et al, 1989). Tsai et al (1983) isolated a new alkaline elastase from alkalophilic Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

Effects of an alkaline elastase from an alkalophilic Bacillus strain on the tenderization of beef meat

Takagi¹,

Kondou²,

Hisatsuka³

et al. 1992

J. Agric. Food Chem.

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Section: Introductionmentioning

confidence: 99%

Effects of an alkaline elastase from an alkalophilic Bacillus strain on the tenderization of beef meat

Takagi¹,

Kondou²,

Hisatsuka³

et al. 1992

J. Agric. Food Chem.

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“…The bacterium was isolated from a batch of South African cured hides whose bacterial population possessed a high collagenolytic activity (Woods, Welton, Thomson & Cooper, 1972 Collagenolytic activity assays. Collagenolytic activity was measured by determining released amino acids, expressed as pmoles glycine/ml, by the method of Adamcic & Clark (I 970).…”

Section: E T H O D Smentioning

confidence: 99%

Section: E T H O D Smentioning

confidence: 99%

Halotolerant Collagenolytic Activity of Achromobacter iophagus

Welton

Woods

1973

Journal of General Microbiology

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A strain of Achromobacter iophagus isolated from cured hides was shown to lyse collagen rapidly under aerobic conditions. Changes of temperature, pH, NaCl or collagen concentration affected either the maximum rate of collagen lysis or the lag before this rate was attained, or both. Collagenolytic activity occurred in 0.85 to 1 0 % (w/v) NaCI. Collagenolytic activity by hide bacteria is regarded as the cause of leather decay and thus a knowledge of the conditions under which these bacteria can degrade collagen is important to the hide and skin industry. The present study of a vigorously collagenolytic hide bacterium aimed to determine the optimal conditions for collagenolytic activity with a view to purification of the collagenase. I N T R O D U C T I O N M E T H O D SAll percentage compositions are wiv and all nutrients are Difco (Detroit, Michigan, U.S.A.) unless stated otherwise.Source and identification. The bacterium was isolated from a batch of South African cured hides whose bacterial population possessed a high collagenolytic activity (Woods, Welton, Thomson & Cooper, 1972 (Skerman, I 967).Media. The bacterium was maintained on a complex medium containing (g/l): casein hydrolysate (British Drug Houses, Poole, Dorset and Merck AG, Darmstadt, Germany), 17.0; glucose, 5.0; glycerol, 10.0; NaCI, 23.4; Na,SO,, 0 . 1 ; nutrient broth, 8.0; soytone, 3.0; tryptone, 0.5; vitamin-free Casamino acids, 0.5; yeast extract, 2-0; and agar, 15.0. The pH was adjusted to 7.6 with NaOH. Owing to the rapid spreading of the bacterium, this medium was not suitable for isolating clones. Discrete colonies were obtained on a medium consisting of: minimal salts solution, 125 ml; glucose, 2 g; agar, 15 g; distilled water to I 1. The minimal salts solution contained (g/l) : KH,PO,, 8 ; K,HPO,, 24; MgS04. 7H20, 0.8 ; Na,SO, (anhydrous), 16; NH,CI, 40; and NH,NO,, 8.

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Some newly characterized collagenases from procaryotes and lower eucaryotes

Keil¹

1979

Mol Cell Biochem

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Chemical and enzymatic properties of four collagenases newly isolated from anaerobic Clostridium histolyticum, aerobic Achromobacter iophagus, and from two lower eucaryotes, the fungus Entomophthora coronata and the insect Hypoderma lineatum are reviewed. The problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in Achromobacter by their macromolecular substrates are discussed. The two bacterial collagenases are Zn-metallo-enzymes; the highly purified Clostridium collagenase contains cyst(e)ine, serine phosphate and tryptophan additionally to amino acids reported previously. Achromobacter collagenase has the highest specific activity of all collagenases; it yields by autolysis enzymatically active degraded forms. The active dimer is composed of two identical subunits of molecular weight 35,000. Similarities between Achromobacter collagenase, thermolysin and Bacillus subtilis neutral proteinase in molecular weight, amino acid composition, and amino acids important for the active sites are discussed. The two collagenases from low eucaryotes are serine proteinases; Hypoderma collagenase is homologous to the trypsin family in the amino terminal sequence. The initial cleavage of native collagen by highly purified bacterial collagenases occurs in the central helical part of the alpha chains and not progressively from the amino terminal end. One of the two initial cleavages produced by Achromobacter collagenase is situated in the region cleaved specifically by vertebrate collagenases, but with different bond specificity. The same is true for the insect collagenase. Entomophthora collagenase is a proteinase of broad specificity which also cleaves collagen in its helical parts. All four collagenases also degrade other proteins according to their bond specificity.

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Collagenolytic Activity of Cured Hide Bacteria

Cited by 18 publications

References 4 publications

Effects of an alkaline elastase from an alkalophilic Bacillus strain on the tenderization of beef meat

Effects of an alkaline elastase from an alkalophilic Bacillus strain on the tenderization of beef meat

Halotolerant Collagenolytic Activity of Achromobacter iophagus

Some newly characterized collagenases from procaryotes and lower eucaryotes

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