Purification and characterization of myofibril-bound serine protease from lizard fish (Saurida undosquamis) muscle

Ohkubo, Makoto; Miyagawa, Kourin; Osatomi, Kiyoshi; Hara, Kenji; Nozaki, Yukinori; Ishihara, Tadashi

doi:10.1016/j.cbpc.2003.10.015

Cited by 12 publications

(12 citation statements)

References 36 publications

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“…The enzymes are classified as serine proteinase and tightly bound to myofibril. Dissociation of these enzymes from myofibril is achieved by either heat or acid treatments at pH 4-5 or combination of both (Ohkubo et al, 2004;Cao et al, 2004Cao et al, , 2005. These enzymes are believed to be responsible for textural degradation of myofibrillar proteins including myosin heavy chain, actin, and tropomyosin of washed mince (Cao et al, 2005).…”

Section: Resultsmentioning

confidence: 99%

Gelation Characteristics of Mince and Washed Mince From Small-Scale Mud Carp and Common Carp

Yongsawatdigul

Pivisan

Wongngam

et al. 2013

Journal of Aquatic Food Product Technology

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Small-scale mud carp (SC, Cirrhina microlepis) and common carp (CC, Cyprinus carpio) are underutilized freshwater fish. The objective of this study was to elucidate the gel-forming ability of mince and washed mince from these species in relation to washing cycles and CaCl 2 addition. Protein loss of up to 67% was observed after three-washing cycles of both species, rendering relatively low yield. About 85-90% of total fat was removed from SC flesh after three-washing cycles, but only two-washing cycles were sufficient for fat removal in CC mince. Mince and washed mince of both species did not exhibit severe proteolysis with low autolytic activity at 65 • C. SC exhibited superior gel-forming ability to CC. Two-and three-washing cycles in conjunction with a 40 • C-preincubation resulted in the highest textural properties of SC and CC, respectively. CaCl 2 increased the breaking force of CC and SC mince gels up to 65 and 95% at 0.3 and 0.5% CaCl 2 , respectively, as compared to without CaCl 2 . However, it showed negative effects on surimi gels of both species. Both SC and CC are potential freshwater fish resources for mince and washed mince production with reasonable good gel-forming ability.

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Section: Resultsmentioning

confidence: 99%

Gelation Characteristics of Mince and Washed Mince From Small-Scale Mud Carp and Common Carp

Yongsawatdigul

Pivisan

Wongngam

et al. 2013

Journal of Aquatic Food Product Technology

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“…A new type of serine protease was recently reported, which was a myofibril‐bound serine protease (MBSP) from the muscle myofibril fraction of several fishes including carp ( Cyprinus carpio ), 16 wanieso lizardfish ( Saurida wanieso ), 17 brushtooth lizardfish ( Saurida undosquamis ) 18 and crucian carp ( Carassius giberio langsdorfi ) 19 . Myofibril‐bound serine protease was not dissociated from myofibrils even by detergents, 20 and most degraded myosin heavy chain around 55°C in the presence of 0.5 M NaCl.…”

Section: Introductionmentioning

confidence: 99%

Myofibrillar proteolysis by myofibril-bound serine protease from white croaker Argyrosomus argentatus

et al. 2005

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The modori phenomenon is defined as heat-induced myofibrillar degradation caused by endogenous serine protease(s) of fish muscle during Kamaboko fish meat gel production. This study was undertaken to analyze myofibrillar proteolysis of white croaker Argyrosomus argentatus muscle, which is an ingredient of high quality Kamaboko, by myofibril-bound serine protease (MBSP) under conditions corresponding to the modori phenomenon. White croaker MBSP was stable between pH 2-11 and below 65°C, and about 60% of its initial activity remained after incubation for 2 h under the conditions at 65°C and pH 7.5. About 60% of the enzyme activity was suppressed by 0.5 M NaCl. White croaker MBSP degraded various myofibrillar proteins between 40 and 70°C and pH 6.0-9.0, and preferentially degraded myosin heavy chain rather than other myofibrillar proteins. The enzyme degraded the myosin heavy chain most strongly at 55°C and pH 7.0, and a major part of the bands of myosin heavy chain and its degradation products disappeared for a period of 2 h. These degradation characteristics are very similar to those observed during the modori phenomenon, indicating that MBSP could be a modori-inducing protease involved in the modori phenomenon of white croaker Kamaboko production.

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“…The result was in accordance to Chaijan et al (2013) who reported that MHC and actin were the major protein in frigate mackerel and catfish muscle. Additionally, those major protein components also found in sardine, mackerel (Hashimoto et al, 1979), lizard fish (Ohkubo et al, 2004) and bigeye snapper (Benjakul et al, 2003a). In general, tropomyosin and troponin I with molecular weight about 33 kDa and 20-24 kDa, respectively were also consisted in fish muscle (Benjakul et al, 2011).…”

Section: Degradation Of Nam As Affected By Cpe From Cfmmentioning

confidence: 99%

“…In those cases autolysis was caused by cathepsin L as a typical cysteine protease, while serine proteases were found to be responsible for textural breakdown of threadfin bream (Toyohara and Shimizu, 1988) and oval-filefish . Ohkubo et al (2004) reported that a muscle soluble serine protease (MSSP) purified from the soluble fraction of lizard fish (Saurida undosquamis) muscle could degrade myofibrillar proteins while a collagenolytic serine proteinase (CSP) purified from red sea bream (Pagrus major) skeletal muscle might be involved in the softening of fish muscle, during the post-mortem stage, by degrading MHC (Wu et al, 2010). Moreover, Benjakul et al (2003b) reported that the autolysis of lizardfish caused by myofibril-associated proteinases were both cysteine and serine proteinases.…”

Section: Introductionmentioning

confidence: 99%

Autolysis of Clown Featherback (Chitala ornata) Muscle

Thiabmak¹,

Sriket²,

Yarnpakdee³

et al. 2019

CMUJNS

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Clown featherback (Chitala ornata) is a freshwater fish important in the cuisine of Thailand and other Southeast Asian countries. It has a short marketable life due mainly to poor gelling characteristic even when stored in ice. This deterioration has been associated with muscle autolysis. The research was aimed to investigate the autolysis of clown featherback muscle (CFM). To test autolysis, mince from CFM was incubated in atemperature controlled water bath for 60 min at 5, 10, 20, 30, 40, 50, 60, 65, 70, 75 or 80 °C at pH levels over the range of 2-11. The results showed that the highest autolytic activity was at 70 ºC and it occurred at pH levels of 4 and 7, with pH 4 showing the highest autolysis. A (20.3% inhibition), which had significantly higher inhibitory activity (P<0.05) among the protease inhibitors tested. This suggests that aspartic protease was the major proteinase in CFM. CFM was incubated with its crude enzyme counterpart at the physiological pH (6.73) at both 4 ºC and 25 ºC. Degradation of natural actomyosin showed that after incubation at either temperature myosin heavy chain was susceptible to hydrolysis indicating that autolysis of CFM took place even at low temperature as affected by its endogenous proteases. The effects of several protease inhibitors were tested and autolysis at the physiological pH (6.73) was strongly inhibited by 10 µM pepstatin

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Purification and characterization of myofibril-bound serine protease from lizard fish (Saurida undosquamis) muscle

Cited by 12 publications

References 36 publications

Gelation Characteristics of Mince and Washed Mince From Small-Scale Mud Carp and Common Carp

Gelation Characteristics of Mince and Washed Mince From Small-Scale Mud Carp and Common Carp

Myofibrillar proteolysis by myofibril-bound serine protease from white croaker Argyrosomus argentatus

Autolysis of Clown Featherback (Chitala ornata) Muscle

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