Assay Systems and Characterization of Pacific Whiting (<i>Merluccius productus</i>) Protease

An, Haejung; Seymour, Thomas A.; Wu, Jianbing; Morrissey, Michael T.

doi:10.1111/j.1365-2621.1994.tb06947.x

Cited by 110 publications

(122 citation statements)

References 22 publications

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“…At 60 min, no protein with M r of 36, 22 and 20 kDa were found. An, Seymour, Wu and Morriessey (1994) reported that among the Pacific whiting proteins, MHC was the most extensively hydrolysed by cathepsin L, followed by troponin-T and α-and β-tropomyosin. For the control (without purified proteinase), a slight degradation of 13 myosin heavy chain was observed (lane C) (Fig.…”

Section: Myosinmentioning

confidence: 99%

Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen

et al. 2006

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Trypsin from skipjack tuna (Katsuwonus pelamis) spleen was purified by ammonium sulfate precipitation and a series of chromatographies including Sephacryl S-100 and Benzamidine Sepharose 4 Fast Flow (high sub). The enzyme was purified to 22.3 folds with a yield of 51.6%. The molecular weight of trypsin was estimated to be 42 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified trypsin was able to hydrolyze natural actomyosin (NAM) and myosin, but rarely hydrolyzed collagen. Myosin heavy chain was most susceptible to hydrolysis by trypsin as evidenced by the lowest band intensity remained. The effect of NaCl on proteolytic activity was also studied. The band intensity of myosin heavy chain slightly increased as NaCl concentration increased, suggesting the inhibitory activity of NaCl. When hydrolytic activities of skipjack tuna spleen and bovine pancreas trypsins on sardine proteins, including NAM, myosin and collagen were compared, it was found that trypsin from bovine pancreas showed the greater activity towards NAM and myosin than that from skipjack tuna spleen. However, both enzymes could not degrade collagen.

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Section: Myosinmentioning

confidence: 99%

Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen

et al. 2006

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“…Alcalase was used to hydrolyse gelatin and protease activity was determined as per the method of An et al (1994). The prepared skins were mixed with distilled water at a ratio of 1:10 (w/v).…”

Section: Preparation Of Gelatin Hydrolysatementioning

confidence: 99%

Antioxidant activities and selected characteristics of gelatin hydrolysates from seabass (Lates calcarifer) skin as affected by production processes

et al. 2015

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Antioxidant activities and selected characteristics of gelatin hydrolysates from seabass skin as affected by production processes were investigated. Hydrolysates were prepared using different processes, including hydrolysis during and after gelatin extraction. Samples hydrolysed during gelatin extraction showed a higher degree of hydrolysis (DH) and yield compared with those hydrolysed after gelatin extraction (p<0.05). All hydrolysates had a creamy yellowish colour. A lower abundance of volatile compounds was found in the hydrolysates produced during gelatin extraction, in comparison with those obtained after gelatin extraction. Hydrolysates prepared during gelatin extraction had higher 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, ferric reducing antioxidative power (FRAP) and ferrous ion chelating activity (p<0.05). Following a simulated in vitro gastrointestinal digestion, the DPPH radical scavenging activity and FRAP of the hydrolysates was retained, whilst ferrous ion chelating activity increased. The most appropriate conditions for the generation of antioxidant hydrolysates from seabass skin were identified.

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“…Proteinase activity of spleen extract from each tuna was determined using casein as a substrate according to the method of An et al [31] with a slight modification. To initiate the reaction, 200 µl diluted spleen extract (500 folds) was added into assay mixtures containing 2 mg of casein, 200 µl of distilled water and 625 µl of assay buffer (0.1 M glycine-NaOH, pH 9.0).…”

Section: Enzyme Assaymentioning

confidence: 99%

Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems

Klomklao

Benjakul

Visessanguan

et al. 2005

Process Biochemistry

102

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Partitioning of spleen proteinase from yellowfin tuna (Thunnus albacores) in an aqueous two-phase system (ATPS) was investigated. Phase compositions including PEG molecular mass and concentration as well as types and concentration of salts affected the protein partitioning. ATPS comprising PEG1000 (15% w/w) and magnesium sulfate (20% w/w) provided the best condition for the maximum partitioning of the proteinase into the top phase and gave a highest specific activity (47.0 units/µg protein) and purification fold (6.61). The yield of 69.0% was obtained.Under the same ATPS condition used, the partitioning of proteinase of splenic extract from three tuna species involving skipjack tuna, yellowfin tuna and tongol tuna were compared. The purity of splenic extract from all tuna species increased after ATPS process. Among all species tested, yellowfin tuna showed the highest purification fold, followed by tongol tuna and skipjack tuna, respectively. SDS-substrate gel electrophoresis revealed that the band intensity of major proteinase in ATPS fraction from all tuna species slightly increased with the concomitant decrease in band intensity of other contaminating proteins, indicating the greater specific activity of splenic extract. Therefore, ATPS was an effective method for partitioning and recovery of proteinases from tuna spleen.

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Assay Systems and Characterization of Pacific Whiting (Merluccius productus) Protease

Cited by 110 publications

References 22 publications

Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen

Proteolytic degradation of sardine (Sardinella gibbosa) proteins by trypsin from skipjack tuna (Katsuwonus pelamis) spleen

Antioxidant activities and selected characteristics of gelatin hydrolysates from seabass (Lates calcarifer) skin as affected by production processes

Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems

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