ArticleJournal, genetic engineering & biotechnology2021
Study on cocoonase, sericin, and degumming of silk cocoon: computational and experimental.
Article in Journal, genetic engineering & biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Molecular, Structural and Functional Characterization of Antheraea mylitta Expressed Cocoonase: An Integrative Approach.The protein journal · 2025Article
- Mimicking Design Scaffolds Based on Nonwoven Biological Materials of Silk Cocoon for Soft Tissue Engineering at the Bone Interfacial Area: Structure, Morphology, and Performance Evaluation Based on In Vitro Testing, and Identification of Applied Biomaterials.ACS applied bio materials · 2025Article
- Development of Biodegradable Bioplastics with Sericin and Gelatin from Silk Cocoons and Fish Waste.Toxics · 2024Article
- Silk fibroin-based scaffolds for tissue engineering.Frontiers in bioengineering and biotechnology · 2024Review
- A novel method for silkworm cocoons self-degumming and its effect on silk fibers.Journal of advanced research · 2023Article
- In silico structural and functional characterization of Antheraea mylitta cocoonase.Journal, genetic engineering & biotechnology · 2022Article
- Effects of trypsin-induced limited hydrolysis on the structural, functional, and bioactive properties of sericin.RSC advances · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
backgroundCocoonase is a proteolytic enzyme that helps in dissolving the silk cocoon shell and exit of silk moth. Chemicals like anhydrous Na
resultsPredicted normalized B-factors of cocoonase and sericin with respect to α and β regions showed that these regions are structurally more stable in cocoonase while less stable in sericin. Conserved domain analysis revealed that B. mori cocoonase contains a trypsin-like serine protease with active site range 45 to 180 query sequences while substrate binding site from 175 to 200 query sequences. SDS-PAGE analysis of cocoonase indicated its molecular weight of 25-26 kDa. Na
conclusionsPresent study enlightens on the detailed characteristics of cocoonase and sericin proteins, comparative degumming activity, and image analysis of cocoonase enzyme and Na
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Registered trials
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