Biochemical characterisation of chymotrypsin from the midgut gland of yellowleg shrimp, Penaeus californiensis

Navarrete-del-Toro, Maria A.; García‐Carreño, Fernando; Hernández-Cortés, Patricia; Molnár, Tamás; Gráf, László

doi:10.1016/j.foodchem.2014.09.160

Cited by 19 publications

(28 citation statements)

References 31 publications

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“…) and 35.7 for Penaeus californiensis (Navarrete‐del‐Toro et al . ). The result was in accordance with inhibitor study, which indicated that serine protease (trypsin and chymotrypsin) were present in both AP and MP (Table ).…”

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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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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Section: Resultsmentioning

confidence: 97%

“…) and Penaeus californiensis (Navarrete‐del‐Toro et al . ) contained serine proteases as the dominant enzymes. Furthermore, EDTA, which chelates the metal ions required for the enzyme, was able to partially lower proteolytic activity (31.76 and 25.14% inhibition for AP and MP, respectively).…”

Section: Resultsmentioning

confidence: 99%

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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“…Type Ib brachyurins (crustacean chymotrypsins) share the specificity of type Ia brachyurins, but with a drastic reduction of trypsin activity. Also, collagenolytic serine proteases from L. vannamei are able to digest native porcine type I collagen ( Burgos-Hernández et al 2005 ) as reported for chymotrypsin from another shrimp species, Penaeus californiensis ( Navarrete-del-Toro et al 2015 ). Trypsins from the warm water shrimp Penaeus monodon also have collagenolytic activity in addition to the typical specificity of trypsin ( Lu et al 1990 ), although a further study suggested that this may occur by activation of procollagenase in the native collagen ( Chen et al 1991 ).…”

Section: Crustacean Proteases and Their Debridement Potentialmentioning

confidence: 86%

Crustacean Proteases and Their Application in Debridement

Perera

Rodríguez-Viera

Montero-Alejo

et al. 2020

TLSR

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Digestive proteases from marine organisms have been poorly applied to biomedicine. Exceptions are trypsin and other digestive proteases from a few cold-adapted or temperate fish and crustacean species. These enzymes are more efficient than enzymes from microorganism and higher vertebrates that have been used traditionally. However, the biomedical potential of digestive proteases from warm environment species has received less research attention. This review aims to provide an overview of this unrealised biomedical potential, using the debridement application as a paradigm. Debridement is intended to remove nonviable, necrotic and contaminated tissue, as well as fibrin clots, and is a key step in wound treatment. We discuss the physiological role of enzymes in wound healing, the use of exogenous enzymes in debridement, and the limitations of cold-adapted enzymes such as their poor thermal stability. We show that digestive proteases from tropical crustaceans may have advantages over their cold-adapted counterparts for this and similar uses. Differences in thermal stability, auto-proteolytic stability, and susceptibility to proteinase inhibitors are discussed. Furthermore, it is proposed that the feeding behaviour of the source organism may direct the evaluation of enzymes for particular applications, as digestive proteases have evolved to fill a wide variety of feeding habitats, natural substrates, and environmental conditions. We encourage more research on the biomedical application of digestive enzymes from tropical marine crustaceans.

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“…; Navarrete‐del‐Toro et al . ). The cathepsin D1 of clawed lobster, H. americanus , lacks the poly‐proline loop and β‐hairpin that are present in the bovine homolog, characteristics that seems to allow crustacean cathepsin D1 to digest (Rojo et al .…”

Section: Inborn Characteristics Of Crustacean Peptidasesmentioning

confidence: 97%

The toolbox for protein digestion in decapod crustaceans: a review

Toro¹,

García‐Carreño²

2018

Reviews in Aquaculture

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Pancrustacea, including both crustaceans and insects, is the most abundant and diverse clade of Animalia and occupy all types of environments. They are studied because of their ecological, agricultural, health and economic issues, some being delicatessens. Crustaceans evolved during the Cambrian, thanks to adaptations, such as macrophagy, that allowed them to prey on diverse and energy-rich foods, which depended on complex digestive systems that drove evolution. As heterotrophs, crustaceans depend on their ability to obtain nutrients to fulfil their material, mostly carbon and energy requirements. Protein is the most important nutrient; up to 70% dry mass of a crustacean is protein. Hence, food protein is needed to obtain free amino acids to synthesize protein de novo (from scratch), because animals cannot synthesize the ten essential amino acids de novo. The ability to digest protein must have emerged early in evolution, as shown by the finding of trypsin coding genes in eubacterial genomes. Primitive organisms selectively fixed the ability to use foreign protein as a source of amino acids by synthesizing enzymes, now termed peptidases, which were capable of recognizing and hydrolysing peptide bonds in a specific region of a polypeptide chain, based on specificity for the side chains of amino acid residues in the carboxylic side of the site of cleavage. Here, we present a brief history on what and how digestive peptidases in crustaceans became known.

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Biochemical characterisation of chymotrypsin from the midgut gland of yellowleg shrimp, Penaeus californiensis

Cited by 19 publications

References 31 publications

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

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

Crustacean Proteases and Their Application in Debridement

The toolbox for protein digestion in decapod crustaceans: a review

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