Implication of Muscle Alkaline Proteinase in the Textural Degradation of Fish Meat Gel

Makinodan, Yasuo; Toyohara, Haruhiko; Niwa, Eiji

doi:10.1111/j.1365-2621.1985.tb10475.x

Cited by 54 publications

(31 citation statements)

References 22 publications

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“…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.…”

Section: Methodsmentioning

confidence: 99%

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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Section: Methodsmentioning

confidence: 99%

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

Kim

2005

J Food Biochemistry

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“…The shrimp enzyme had an optimum temperature of 60°C and remained partially active even after exposure to 80°C. Apart from exogenous substrates alkaline proteinase is capable of degrading myofibrillar proteins (Lin and Lanier, 1980;Folco et al, 1984) and, therefore, is implicated in the textural degradation of minced fish meat (Deng 1981;Lanier et al, 1981;Makinodan et al, 1985). Although myofibrillar proteins were not used as substrates in the present study, shrimp muscle alkaline proteinasc seemed to be capable of degrading all protein substrates with the exception of bovine serum albumin.…”

Section: Discussionmentioning

confidence: 73%

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

Doke

Ninjoor

1987

Journal of Food Science

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Activities of an alkaline proteinase and an exopeptidase were detected in the muscle of shrimp. Both enzymes could be extracted with unbuffered 0.5% KCI. The shrimp muscle alkaline proteinase, optimally active at pH 8.0 and 6O"C, was partially purified and characterized. The heat stable enzyme had an apparent molecular weight of 250 KDa. Protein substrates such as casein, azocasein, azocoll and hemoglobin were hydrolyzed by the enzyme while it showed no action on bovine serum albumin and the synthetic substrates of proteinases. Active site directed inhibition experiments suggested that the enzyme was a metaldependent serine proteinase. The shrimp exopeptidase cleaving amino acid naphthylamides at pH 6.8 and 40°C exhibited the characteristics of an aminopeptidase because of its susceptibility to bestatin, puromycin and a metal chelator.

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“…Heat‐stable alkaline protease has often been reported to be responsible for textural degradation of surimi gels. Makinodan et al 24 reported that only alkaline protease could act at the pH of meat paste and 60 °C. Alkaline protease from white croaker had optimum activity at 60 °C and pH 8.0 25.…”

Section: Resultsmentioning

confidence: 99%

Recent Progress in Catalysis and Photochemistry for Energy Technologies

Losse

Junge

2010

ChemSusChem

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the international symposium "Catalysis and Photochemistry for Energy Technologies" organized by the section "Sustainable Chemistry" of the German Chemical Society (GDCh) took place in the city of Rostock, Germany. Matthias Beller, the conference chair and head of the Leibniz-Institute for Catalysis (LIKAT), opened the event focused on hydrogen and solar energy technology and welcomed some of the most renowned scientists in this field of research. In the forefront Beller said: "An important aim of this symposium is to bring together scientists working on photochemistry or catalysis to discuss jointly new developments and perspectives in order to find new approaches for future energy supply."Sufficient and sustainable supply of energy is the prerequisite to a high quality of life and at the same time the central challenge of our century. At present, approximately 86% of the energy used is generated from fossil resources. An increasing development and utilization of renewable energy sources is essential for the future. In this respect, the use of solar energy must play a pivotal role. One hour of sunlight is sufficient to cover an entire year of the world's energy demand. To make this energy useable, great potential lies in the photocatalytic water splitting to hydrogen and oxygen. This allows not only a widening of the energetic raw material base, but is also capable of securing the majority of the global energy demand.One of the lecturers in Rostock was Matthias Driess, who focuses on inorganic and organometallic chemistry at the Technical University of Berlin. [1,2] He demonstrated the necessity of interdisciplinary work at the daylight driven water splitting in photosynthesis. "Photosynthesis of plants is a biocatalytic process where water splitting is of central importance. Clarification of the processes of water oxidation and -reduction in plants is for the most researchers of molecular sciences of central interest." At the cluster of excellence "Unifying Concepts in Catalysis" (UniCat) in Berlin not only biocatalysis for hydrogen evolution and biofuel cells are topics, also bioinspired catalysis for oxygen and hydrogen production with inorganic materials and sunlight is under investigation.Until today, hydrogen is mainly produced by steam reforming of hydrocarbons like methane and is basically used in chemical industry. As a potential energy source it has to be produced in a more sustainable manner. Photocatalysis is clearly one of the most promising options. One possibility is the use of metal oxides or sulfides absorbing light and to catalyze water splitting. As "nanopowders" with a definite crystallinity and special dopants they are working at a given pH of an aqueous solution as heterogeneous catalysts. Recent developments show a high potential of this kind of catalysts. Akihiko Kudo from the Tokyo University of Science was confident of this type of catalysts but also made the point that photon energy conversion still is not at a stage of practical use.

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Implication of Muscle Alkaline Proteinase in the Textural Degradation of Fish Meat Gel

Cited by 54 publications

References 22 publications

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

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

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

Recent Progress in Catalysis and Photochemistry for Energy Technologies

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