A novel fibrin(ogen)olytic trypsin-like protease from Chinese oak silkworm (Antheraea pernyi): Purification and characterization

Geng, Peng; Lin, Le; Li, Yuan; Fan, Qi; Wang, Naihong; Song, Lixin; Li, Wenli

doi:10.1016/j.bbrc.2014.01.155

Cited by 18 publications

(11 citation statements)

References 23 publications

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“…This activation and catalytic mechanism is similar to that of mammalian trypsin . In recent years there have been several reports of cocoonase, both in domestic silkworm and wild silk moths, concerning their properties and applications …”

Section: Introductionsupporting

confidence: 52%

“…10 -12 In recent years there have been several reports of cocoonase, both in domestic silkworm and wild silk moths, concerning their properties 13 -16 and applications. 17,18 Cocoonases are significant not only in understanding the physiological and biochemical processes of the silk moth's escape from the cocoon but also in the exploitation of sericin protein.…”

Section: Introductionmentioning

confidence: 99%

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An active recombinant cocoonase from the silkwormBombyx mori: bleaching, degumming and sericin degrading activities

Unajak

Aroonluke

Promboon

2014

J. Sci. Food Agric.

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In this study, we successfully produced the active recombinant BmCoc in P. pastoris with promising functions for the Thai silk degumming process, which includes degumming, sericin degrading and color bleaching activities. Our data clearly indicated that the recombinant enzyme had proteolytic activity on sericin but not on fibroin proteins. The recombinant BmCoc has proven to be suitable for numerous applications in the silk industry.

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Section: Introductionsupporting

confidence: 52%

Section: Introductionmentioning

confidence: 99%

An active recombinant cocoonase from the silkwormBombyx mori: bleaching, degumming and sericin degrading activities

Unajak

Aroonluke

Promboon

2014

J. Sci. Food Agric.

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“…The discovery of duplicate copies of cocoonase with divergent amino acid sequences might lead to the discovery of a protease that is more effective at degumming. Proteases are also useful for medical applications; recent work on the Chinese silkworm cocoonase has shown that it cleaves fibrin and fibrinogen both in vitro and in an animal model of thrombosis [15], demonstrating its utility for studying thrombosis and potentially treating blood clots. As we show below, the heliconiine cocoonases exhibit substantial variation in surface properties ( particularly hydrophobicity), potentially facilitating their diffusion into diverse chemical environments.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary and structural analyses uncover a role for solvent interactions in the diversification of cocoonases in butterflies

et al. 2018

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Multi-omic approaches promise to supply the power to detect genes underlying disease and fitness-related phenotypes. Optimal use of the resulting profusion of data requires detailed investigation of individual candidate genes, a challenging proposition. Here, we combine transcriptomic and genomic data with molecular modelling of candidate enzymes to characterize the evolutionary history and function of the serine protease cocoonase. butterflies possess the unique ability to feed on pollen; recent work has identified as a candidate gene in pollen digestion. was first described in moths, where it aids in eclosure from the cocoon and is present as a single copy gene. In heliconiine butterflies it is duplicated and highly expressed in the mouthparts of adults. At least six copies of are present in and copy number varies across sub-populations. Most genes are under purifying selection, however branch-site analyses suggest genes may have evolved under episodic diversifying selection. Molecular modelling of cocoonase proteins and examination of their predicted structures revealed that the active site region of each type has a similar structure to trypsin, with the same predicted substrate specificity across types. Variation among heliconiine cocoonases instead lies in the outward-facing residues involved in solvent interaction. Thus, the neofunctionalization of duplicates appears to have resulted from the need for these serine proteases to operate in diverse biochemical environments. We suggest that may have played a buffering role in feeding during the diversification of across the neotropics by enabling these butterflies to digest protein from a range of biochemical milieux.

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“…In the study, comparing with other fibrinolytic enzymes [29,31,42], we found that PSLTro01 could also inhibit carrageenan-induced tail thrombosis and the effect was similar to that of urokinase. A lot of fibrinolytic enzymes [7,10,43] not only have antithrombotic effect but also have anticoagulant activity. The blood coagulation cascade includes the intrinsic blood coagulation pathway, extrinsic blood coagulation pathway, and common blood coagulation pathway.…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Tian

Лі

Li-wei

et al. 2015

International Journal of Biological Macromolecules

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A novel fibrin(ogen)olytic trypsin-like protease from Chinese oak silkworm (Antheraea pernyi): Purification and characterization

Cited by 18 publications

References 23 publications

An active recombinant cocoonase from the silkwormBombyx mori: bleaching, degumming and sericin degrading activities

An active recombinant cocoonase from the silkwormBombyx mori: bleaching, degumming and sericin degrading activities

Evolutionary and structural analyses uncover a role for solvent interactions in the diversification of cocoonases in butterflies

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

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