Low molecular weight trypsin from hepatopancreas of freshwater prawn (Macrobrachium rosenbergii): Characteristics and biochemical properties

Sriket, Chodsana; Benjakul, Soottawat; Visessanguan, Wonnop; Hara, Kenji; Yoshida, Asami; Liang, Xiao

doi:10.1016/j.foodchem.2012.02.173

Cited by 36 publications

(49 citation statements)

References 39 publications

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“…As a result, the lowered activity could be attained (Sriket et al . ). At high temperatures, the enzyme more likely underwent denaturation and lost its activity.…”

Section: Resultsmentioning

confidence: 97%

“…; Sriket et al . ). From the inhibitor studies, and pH/temperature profiles, it can be inferred that crude protease from A. vulgaris and M. lanchesteri contained several groups of proteases, but serine proteases, both of trypsin and chymotrypsin‐like enzymes, were prevalent.…”

Section: Resultsmentioning

confidence: 97%

“…Trypsin from hepatopancreas of freshwater prawn ( Macrobrachium rosenbergii ) had a MW of 17 kDa (Sriket et al . ). Wu et al .…”

Section: Resultsmentioning

confidence: 97%

“…), Macrobrachium rosenbergii (Sriket et al . ) and Penaeus californiensis (Navarrete‐del‐Toro et al . ) contained serine proteases as the dominant enzymes.…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Endogenous Protease and the Changes in Proteolytic Activity ofAcetes vulgarisandMacrobrachium lanchesteriDuringKapiProduction

Pongsetkul

Benjakul

Sumpavapol

et al. 2016

Journal of Food Biochemistry

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Characteristics of endogenous proteases of shrimp, Acetes vulgaris (AP) and Macrobrachium lanchesteri (MP) as well as the changes in proteolytic activity during Kapi production were investigated. Maximal activity of AP and MP was found at pH 7, 60C and pH 8, 60C, respectively. Activity of both proteases decreased with increasing NaCl concentration (0–30%). Both extracts were strongly inhibited by N‐ethylmaleimide‐phenylmethane‐sulfonyl fluoride (PMSF) and soybean trypsin inhibitor (SBTI), suggesting that major proteases belonged to serine proteases. This was coincidental with high trypsin activity toward BAPNA and chymotrypsin activity toward BTEE. Proteolytic activity, trypsin and chymotrypsin were detectable throughout Kapi fermentation. The activity was decreased when salting was implemented. Nevertheless, activities increased continuously with increasing fermentation time. During Kapi production, proteins underwent degradation as indicated by the formation of oligopeptides and disappearance of myosin heavy chain and actin. Therefore, both endogenous and microbial proteases were more likely involved in proteolysis of shrimp during Kapi production. Practical Applications Kapi, traditional salted shrimp paste, is usually used as a condiment to enhance the palatability of many Thai foods. Recently, small shrimp Acetes Vulgaris and Macrobrachium lanchesteri have become the new alternative raw materials for Kapi production because of their availability. During fermentation, protein hydrolysis is induced by endogenous proteases in shrimp as well as those produced by halophilic bacteria. Those changes medicated by proteolysis can be associated with the final characteristics of Kapi.

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“…As a result, the lowered activity could be attained (Sriket et al . ). At high temperatures, the enzyme more likely underwent denaturation and lost its activity.…”

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 97%

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Characterization of Endogenous Protease and the Changes in Proteolytic Activity ofAcetes vulgarisandMacrobrachium lanchesteriDuringKapiProduction

Pongsetkul

Benjakul

Sumpavapol

et al. 2016

Journal of Food Biochemistry

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“…The result was in agreement with our previous study, in which both shrimps, A. vulgaris and M. lanchesteri, contained several groups of proteases, but serine proteases were dominant, particularly trypsin or chymotrypsin-like enzymes (Pongsetkul et al, 2016b). Several crustaceans including Penaeus vannamei (Garcia-Carreno et al, 2008), Macrobrachium rosenbergii (Sriket et al, 2012) and Penaeus californiensis (Navarrete-del-Toro et al, 2015), etc. contained serine proteases as the major enzymes.…”

Section: Effect Of Various Protease Inhibitorsmentioning

confidence: 99%

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Pongsetkul¹,

Benjakul²,

Sumpavapol³

et al. 2017

Turk. J. Fish. Aquat. Sci.

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Autolysis of Acetes vulgaris and Macrobrachium lanchesteri was comparatively studied. Maximal autolytic activities were found at pH 7, 55°C for A. vulgaris and pH 8, 60°C for M. lanchesteri. Both shrimps dominantly contained serine proteases as indicated by the marked inhibition by PMSF and SBTI. When both shrimps were used for Kapi production and characterized, differences in characteristics as well as antioxidant activities were obtained. Kapi produced from A. vulgaris (KA) showed the higher degree of hydrolysis (15.93±0.51%), peroxide values (0.20±0.23 mg cumene peroxide/ kg sample) and TBARS value (0.55±0.16 mg MDA/ kg sample), compared with Kapi produced from M. lanchesteri (KM), indicating the higher protein degradation and lipid oxidation in this sample. Moreover, KA also possessed the higher antioxidative activities including ferric reducing antioxidant power (FRAP) (14.12±1.34 µmol TE/ g sample), chelating activity (3.21±0.05 µmol EE/ g sample), hydrogen peroxide (30.05±0.49 µmol TE/ g sample) and singlet oxygen scavenging activities (48.46±0.32 µmol EE/ g sample) than KM, except for DPPH and ABTS radical scavenging activities, which showed lower activity (P<0.05) and had no difference (P>0.05), respectively. Therefore, different levels and types of endogenous proteases in both shrimps determined the autolysis, characteristics and antioxidative properties of resulting Kapi.

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