Characteristics of an alkaline proteinase and exopeptidase from shrimp (<i>Penaeus indicus</i>) muscle

Doke, S. N.; Ninjoor, V.

doi:10.1111/j.1365-2621.1987.tb14044.x

Cited by 21 publications

(17 citation statements)

References 32 publications

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“…2a). Doke and Ninjoor (1987) have also reported the presence of an alkaline metal dependent serine protease, with activity at pH 7 in shrimp ( Penaeus indicus ).…”

Section: Resultsmentioning

confidence: 95%

Chemical and microbial quality indexes of Norwegian lobsters (Nephrops norvegicus) dusted with sulphites

Martínez-Álvarez

Gómez‐Guillén

Montero³

2008

Int J of Food Sci Tech

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Running title: Quality of Norwegian lobsters dusted with sulphites. AbstractThe effect of dusting with a commercial sulphite-based anti-melanosis formulation on several chemical quality indexes of Norwegian lobsters (Nephrops norvegicus) was evaluated and compared with a control batch during iced storage. Dusting with 6% of the commercial product did not exceed the SO 2 residual levels permitted by the EU Directive and by the Food and Drug Administration. The additive retarded successfully the occurrence of black spots on the crustacean surface for at least 7 days and also bleached the samples. The prior addition of the sulphite-based compound did not affect either muscle pH or total volatile basic nitrogen content during storage, although it did produce increased lipid oxidation. The protease activity decreased, and differences in the pool composition of proteases were observed, serine and cysteine protease activities showing an increase. Finally, the sulphite-based compound delayed agmatine production and exerted an antimicrobial effect on H 2 S-producers and Enterobacteria.

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“…2a). Doke and Ninjoor (1987) have also reported the presence of an alkaline metal dependent serine protease, with activity at pH 7 in shrimp ( Penaeus indicus ).…”

Section: Resultsmentioning

confidence: 95%

Chemical and microbial quality indexes of Norwegian lobsters (Nephrops norvegicus) dusted with sulphites

Martínez-Álvarez

Gómez‐Guillén

Montero³

2008

Int J of Food Sci Tech

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“…2000). The B. subtilis JM‐3 protease did not hydrolyze BTEE, which was the specific substrate for chymotrypsin‐like proteases (Doke and Ninojoor 1987; Choi et al. 1999b).…”

Section: Resultsmentioning

confidence: 99%

“…2005). The B. subtilis JM‐3 protease was not inhibited by 1‐mM NEM and PCMB, which were specific inhibitors for cysteine proteases (Doke and Ninojoor 1987), and by EDTA, which was the specific inhibitor for metalloproteases (Oliveria et al. 2005).…”

Section: Resultsmentioning

confidence: 99%

“…The effect of the substrates on enzyme activity was determined by adding 250 μL of enzyme solution to 250 μL of 1 mM or 1% substrates; azocasein (Ninojoor and Srivastava 1985), casein (Makinodan et al. 1985), BSA (Doke and Ninojoor 1987), N‐α‐benzoyl‐L‐Arg‐p‐nitroanilide (Oliveria et al. 2005) and p‐tosyl‐L‐arginine methyl ester (TAME), benzoyl‐L‐tyrosine ethyl ester (BTEE), benzyloxycarbonyl‐glycine‐p‐nitrophenyl ester (Z‐Gly‐ONp), benzyloxycarbonyl‐L‐alanine‐p‐nitrophenyl ester (Z‐L‐Ala‐ONp) (Erlanger et al.…”

Section: Methodsmentioning

confidence: 99%

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Purification and Characterization of Bacillus Subtilis Jm-3 Protease From Anchovy Sauce

Kim

2005

J Food Biochemistry

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Bacillus subtilis JM‐3 was isolated from anchovy sauce naturally fermented in an underground cellar at 15 ± 3C for 3 years. The activity of the B. subtilis protease was highest in the 40–60% ammonium sulfate fraction. The yield of the purified protease was 5.3%, and its purification ratio was 35.6 folds. The molecular weight of the B. subtilis protease was 17.1 kDa, and its Km and Vmaxvalues were 1.75 μg/mL and 318 μM 1/min, respectively. The optimal temperature for protease activity was 60C, but optimal stability temperature was 30C. The optimal pH for protease activity and stability was 5.5. Therefore, the B. subtilis JM‐3 protease was classified as an acid protease. The relative activities of the B. subtilis JM‐3 protease were 69, 21 and 1.3% at 10, 20 and 30% NaCl concentrations, respectively. The best substrate for the B. subtilis JM‐3 protease was benzyloxycarbonyl‐glycine‐p‐nitrophenyl ester followed by bovine serum albumin. p‐Toluene‐sulfonyl‐L‐lysine chloromethylketone was the strongest inhibitor followed by soybean trypsin inhibitor, but N‐ethylmaleimide did not inhibit this enzyme. The B. subtilis JM‐3 protease was therefore presumed to be a trypsin‐like serine protease.

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“…3) were alkaline proteases. Previously Doke and Ninjoor (1987) reported that cathepsin B, H and alkaline proteases in shrimp muscle hydrolyzed casein, hemoglobin and benzoyal-Arg-β-napthalamide. Ezquerra et al (1999) reported Leu-, Gly-, Ala-, Val-, Met-, Pro-and Arg-amonipeptidase activities of extracts of white shrimp hepatopancreas.…”

Section: Resultsmentioning

confidence: 99%

Distribution of Proteolytic Activity in the Different Protein Fractions of Tropical Shrimp Head Waste

2008

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Ammonium sulfate fractionated protein fractions at levels of 25%, 30%, 35%, 40%, 42.5% and 45% ammonium sulfate were recovered from the head waste of tropical marine tiger (MTS), culture tiger (CTS), white (WS) and brown shrimp (BS) and then characterized for protease activity. Distribution of buffer (pH 7.1) extracted protein among ammonium sulfate fractions showed that total protein in 25% fraction of MTS, CTS, WS and BS was 48, 54, 34 and 24 times more than that in the respective 42.5% fraction of the head waste of these shrimps. The highest proteolytic activity was observed in 42.5% (NH 4 ) 2 SO 4 protein fraction of the head waste of MTS, CTS, WS and BS, the values were 19, 1.7, 11.6 and 2 times, respectively, more than that of the corresponding 25% (NH 4 ) 2 SO 4 protein fractions. Highest caseinolytic activity (pH 8.5) and gelatinolytic activity (pH 7.1) was observed in the 42.5% fraction of the head waste of CTS and WS, respectively; but the highest albuminolytic activity (pH 8) was observed in the same fraction of the head waste of both MTS and BS. The optimum pH for highest gelatinolytic and albuminolytic activity of the 42.5% (NH 4 ) 2 SO 4 protein fraction of the head waste of MTS and BS was 4; the same for highest gelatinolytic activity of the same protein fraction of the head waste of WS, and these fractions included acid proteases such as pepsin, the optimum pH for the above activity of the same fraction of CTS was 6-8.5, and the fraction was an alkaline protease such as chymotrypsin. The SDS-PAGE pattern of 42.5% (NH 4 ) 2 SO 4 protein fraction of the head waste of BS, CTS, WS and MTS was almost similar with a dark band close to the marker band 20kDa. Proteases make up to 48% of industrial enzymes and are mostly used in detergents, leather production and food industry.

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Characteristics of an alkaline proteinase and exopeptidase from shrimp (Penaeus indicus) muscle

Cited by 21 publications

References 32 publications

Chemical and microbial quality indexes of Norwegian lobsters (Nephrops norvegicus) dusted with sulphites

Chemical and microbial quality indexes of Norwegian lobsters (Nephrops norvegicus) dusted with sulphites

Purification and Characterization of Bacillus Subtilis Jm-3 Protease From Anchovy Sauce

Distribution of Proteolytic Activity in the Different Protein Fractions of Tropical Shrimp Head Waste

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