Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle

Benjakul, Soottawat; Visessanguan, Wonnop; Leelapongwattana, Kittima

doi:10.1016/s1096-4959(02)00290-7

Cited by 32 publications

(30 citation statements)

References 36 publications

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“…This possibly indicated the presence of myofibrilar associated proteinase that bound tightly with NAM and could not be removed during extraction process. Fish muscle was reported to contained myofibril bound proteinases (Benjakul, Visessanguan & Leelapongwattana, 2003 …”

Section: Hydrolysis Of Different Protein Substrates By Purified Trypsmentioning

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: Hydrolysis Of Different Protein Substrates By Purified Trypsmentioning

confidence: 99%

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

et al. 2006

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“…Difference in inhibitory activity of CPP toward the proteinases from the two different species is likely due to differences in the type(s) and amount(s) of proteinase(s) predominantly found in the sarcoplasmic fluid. Benjakul et al (2003c) reported that major sarcoplasmic proteinase in bigeye snapper was heat-activated alkaline proteinase, classified as a serine proteinase. It had an optimum temperature at 60°C.…”

Section: Inhibitory Activity Of Cpp On Sarcoplasmic Proteinasesmentioning

confidence: 99%

“…Fish mince contains both sarcoplasmic proteinases and myofibril-associated proteinases. As a consequence, higher autolysis generally occurs in mince, compared to washed mince in which sarcoplasmic proteinase has been removed (Benjakul et al, 2003c). Since sarcoplasmic proteinases were inhibited effectively by CPP, especially at a higher concentration (Table 1), autolysis caused by sarcoplasmic proteinases in mince was reduced.…”

Section: Inhibitory Activity Of Cpp On the Autolysis Of Mince And Wasmentioning

confidence: 99%

“…For mince and washed mince without CPP addition (lane 2), MHC band intensity decreased considerably after incubation at elevated temperature. The degradation was attributed to endogenous proteinases, which are activated at high temperature normally ranging from 60 to 65°C (Benjakul et al, 2003c). Cao, Osatomi, Hara, and Ishihara (2000) reported that a serine myofibril-bound proteinase in lizardfish, with a molecular mass of 29 kDa, hydrolyzed MHC at 55-60°C.…”

Section: Inhibitory Activity Of Cpp On the Autolysis Of Mince And Wasmentioning

confidence: 99%

“…Alkaline proteinases are also implicated in some fish species (Boye & Lanier, 1988;Lin & Lanier, 1980). Recently, Benjakul, Visessanguan, and Leelapongwattana (2003c) reported that heat-activated alkaline proteinase in bigeye snapper played an important role in degradation of muscle protein, especially at 60-65°C. The sarcoplasmic proteinase which contributes to poor gel forming ability of lizardfish (Saurida tumbil) muscle (Benjakul, Visessanguan, & Turksuban, 2003a) is also a heat-activated alkaline proteinase with an optimum pH and temperature of 8.0 and 65°C, respectively (Benjakul, Visessanguan, & Turksuban, 2003b).…”

Section: Introductionmentioning

confidence: 99%

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Characterisation of proteolytic enzymes from muscle and hepatopancreas of fresh water prawn (Macrobrachium rosenbergii)

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Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle

Cited by 32 publications

References 36 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

Chicken plasma protein: Proteinase inhibitory activity and its effect on surimi gel properties

Characterisation of proteolytic enzymes from muscle and hepatopancreas of fresh water prawn (Macrobrachium rosenbergii)

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