First Report of the Cymbidium Mosaic Potexvirus (CymMV) Infecting the Terrestrial Orchid Phaius tankervilliae in Costa Rica

In 1996, plants of the terrestrial orchid Phaius tankervilliae from a nursery in the Central Valley of Costa Rica were observed with mild to severe foliar symptoms of chlorotic streak. No differences were observed in growth, bulb production, flowers, or flowering time between symptomatic and asymptomatic plants, except the symptomatic plants had earlier senescence. Occasionally, the flowers displayed symptoms of chlorosis and white rings in the sepals. Extracts from symptomatic leaves were concentrated by differential centrifugation and analyzed after sucrose gradients. Negative staining of fractions from gradients from symptomatic plants showed the presence of filamentous viral particles 500 by 17 nm. Purified particles contained a single major protein of about 28 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a single RNA of about 7 kb, which is greater than the 6.2 kb reported (GenBank). These data suggest the presence of a potexvirus in symptomatic plants (1,2). In enzyme-linked immunosorbent assays, symptomatic plants reacted strongly with antiserum specific for Cymbidium mosaic potexvirus (CymMV). This is the first report of CymMV in P. tankervilliae in Costa Rica. References: (1) J. A. Frowd and J. H. Tremaine. Phytopathology 67:43, 1977. (2) H. T. Hsu et al. Phytopathology 82:491, 1992.

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A metalloproteinase extracellularly released byCrithidia deanei

Canadian Journal of Microbiology ◽

10.1139/w03-081 ◽

2003 ◽

Vol 49 (10) ◽

pp. 625-632 ◽

Cited By ~ 15

Author(s):

Claudia Masini d'Avila-Levy ◽

Rodrigo F Souza ◽

Rosana C Gomes ◽

Alane B Vermelho ◽

Marta H Branquinha

Keyword(s):

Molecular Mass ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Gel Filtration ◽

Residual Activity ◽

Major Protein ◽

Motile Cells ◽

Sds Page ◽

Triton X

Actively motile cells from a cured strain of Crithidia deanei released proteins in phosphate buffer (pH 7.4). The molecular mass of the released polypeptides, which included some proteinases, ranged from 19 to 116 kDa. One of the major protein bands was purified to homogeneity by a combination of anion-exchange and gel filtration chromatographs. The apparent molecular mass of this protein was estimated to be 62 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDSPAGE). The incorporation of gelatin into SDSPAGE showed that the purified protein presented proteolytic activity in a position corresponding to a molecular mass of 60 kDa. The enzyme was optimally active at 37 °C and pH 6.0 and showed 25% of residual activity at 28 °C for 30 min. The proteinase was inhibited by 1,10-phenanthroline and EDTA, showing that it belonged to the metalloproteinase class. A polyclonal antibody to the leishmanial gp63 reacted strongly with the released C. deanei protease. After Triton X-114 extraction, an enzyme similar to the purified metalloproteinase was detected in aqueous and detergent-rich phases. The detection of an extracellular metalloproteinase produced by C. deanei and some other Crithidia species suggests a potential role of this released enzyme in substrate degradation that may be relevant to the survival of trypanosomatids in the host.Key words: endosymbiont, trypanosomatid, extracellular, proteinase.

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Natural Occurrence of Chilli veinal mottle virus on Capsicum chinense in China

Plant Disease ◽

10.1094/pd-90-0377c ◽

2006 ◽

Vol 90 (3) ◽

pp. 377-377 ◽

Cited By ~ 8

Author(s):

J. Wang ◽

Z. Liu ◽

S. Niu ◽

M. Peng ◽

D. Wang ◽

...

Keyword(s):

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Viral Disease ◽

Mottle Virus ◽

Major Protein ◽

Natural Occurrence ◽

Capsicum Chinense ◽

Thin Sections ◽

First Report ◽

Chilli Veinal Mottle Virus

An outbreak of a viral disease on chili pepper (Capsicum chinense Jacp. cv. Yellow Lantern) occurred in Hainan Province, China during 2003 and 2004. The disease was prevalent in five chili-producing counties surveyed. Leaves of infected plants initially displayed symptoms of dark green banding along veins and later became distorted with striking mosaic. Infected plants had reduced flower numbers and fruit set, resulting in a significant yield loss. The causative virus was characterized and identified as Chilli veinal mottle virus (ChiVMV) (3). An isolate of the virus was obtained via three single lesion passages through Chenopodium amaranticolor and was shown to reproduce the same symptoms on inoculated C. chinense cv. Yellow Lantern. Negative staining of crude extracts of the infected tissue and subsequent electron microscopy revealed flexuous rods of 12 to 13 × 750 nm, typical of a potyvirus. Pinwheel-like inclusion bodies were abundant in thin sections of infected leaves. Purified virus preparations contained one major protein of 32.8 kDa and one minor protein of 28 kDa when fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both of these protein bands were excised and subsequently analyzed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Multiple peptide fragments from both proteins were identified as arising from ChiVMV capsid protein (CP) (1,2). Therefore, the 32.8-kDa protein is the full-length ChiVMV CP and the 28-kDa protein is presumably a degradation product of the CP. The combined biological and molecular data provided strong evidence that the viral disease on C. chinense was caused by ChiVMV. To our knowledge, this is the first report of ChiVMV infection on C. chinense in China and the first report of C. amaranticolor as an experimental host for ChiVMV. References: (1) P. Chiemsombat et al. Arch. Virol. 143:1855, 1998. (2). J. Joseph and H. S. Savithri. Arch. Virol. 144:1679, 1999. (3) P. Siriwong et al. Plant Pathol. 44:718, 1995.

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Plasma protein concentrations of the young and adult Amazona brasiliensis parrots

Veterinarski glasnik ◽

10.2298/vetgl170117008s ◽

2017 ◽

Vol 71 (1) ◽

pp. 44-51

Author(s):

Elizabeth Schmidt ◽

Patricia Serafini ◽

Elenise Sipinski ◽

Antonio Paulillo

Keyword(s):

Plasma Protein ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Clinical Pathology ◽

Specific Protein ◽

Major Protein ◽

Plasma Protein Concentration ◽

Protein Gel ◽

Sds Page

Introduction. The Red-tailed Amazon parrot (Amazona brasiliensis) is an endangered species of the Psittacine family, and for which various data are important for a comprehensive preservation plan. Data about plasma protein gel electrophoresis of Amazon parrot blood are scarce. The purpose of this study was to determine plasma protein concentrations and concentrations of major protein bands in blood of young and adult Red-tailed Amazon parrot (Amazona brasiliensis). Materials and Methods. Blood samples from eight young and eight adult healthy free-living parrots were obtained. Plasma protein concentration and fractions were determined using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Mann-Whitney U test was used to compare variables. Results and Conclusions. Six major protein bands with the following molecular weights were identified by SDS-PAGE: 170 kDa, 117 kDa, 85 kDa (putative ovotransferrin), 60 kDa, 45 kDa and 23 kDa. Adult parrots had significantly higher concentrations of total proteins, albumin and other proteins with similar mobility (around 60 kDa). Young birds had significantly higher levels of 23kDa proteins. The concentration of putative ovotransferrin (85 kDa) was not different between young and adult parrots. Plasma protein gel electrophoresis patterns in Red-tailed Amazon parrots are similar between young and adult animals, but specific protein bands differ in their absolute concentrations. This finding should be taken into consideration when clinical pathology data are analysed.

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Pheromaxein, the pheromonal steroid-binding protein, is a major protein synthesized in porcine submaxillary salivary glands

Journal of Endocrinology ◽

10.1677/joe.0.1280205 ◽

1991 ◽

Vol 128 (2) ◽

pp. 205-212 ◽

Cited By ~ 5

Author(s):

W. D. Booth ◽

K. I. von Glos

Keyword(s):

Total Protein ◽

Binding Protein ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Submaxillary Gland ◽

Major Protein ◽

Sds Page ◽

Gland Tissue ◽

Steroid Binding ◽

Steroid Binding Protein

ABSTRACT Submaxillary salivary gland tissue from large White, Göttingen miniature and Meishan (Chinese) breeds of pig, and European wild boars, was incubated with [35S]methionine. The radiolabelled amino acid was incorporated into protein in all incubations as demonstrated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Specifically [35S]methionine was predominantly incorporated into the α- and β-charge isomers of pheromaxein, a 16-androstene steroid-binding protein, as shown by SDS-PAGE in combination with vertical isoelectric focusing on polyacrylamide slab gels. The synthesis of pheromaxein occurred in submaxillary gland tissue from both sexes, including tissues stored frozen at −70 °C for long periods. There was little evidence for pheromaxein synthesis in parotid gland tissue or skeletal muscle. Total protein, pheromaxein and total 16-androstenes were determined in the submaxillary gland cytosols of six mature Göttingen miniature boars and a positive correlation was found between these glandular constituents. The amounts of endogenous pheromaxein relative to total protein in the submaxillary gland cytosols (range 10·3–18·0%), together with the predominant synthesis of this protein in vitro, indicate that pheromaxein is a major protein produced in porcine submaxillary glands, particularly in those of the male. Journal of Endocrinology (1991) 128, 205–212

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Myeloperoxidase: its structure and expression during myeloid differentiation

Blood ◽

10.1182/blood.v65.2.484.484 ◽

1985 ◽

Vol 65 (2) ◽

pp. 484-491 ◽

Cited By ~ 116

Author(s):

HP Koeffler ◽

J Ranyard ◽

M Pertcheck

Keyword(s):

Relative Rate ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Major Protein ◽

Trichloracetic Acid ◽

Major Band ◽

Minor Band ◽

Sds Page ◽

Human Granulocytes ◽

Normal Human

Abstract Myeloperoxidase (MPO) is a major protein present in myeloid cells and is used by these cells to help kill microbes. The human promyelocytic HL-60 line can be induced to differentiate to granulocytes or macrophagelike cells. Poly (A) containing RNA was isolated from HL-60 granulocytes, HL-60 macrophages, HL-60 blasts, and normal human granulocytes. The mRNA was translated in a reticulocyte lysate system in the presence of 35S-methionine. The MPO was precipitated from the lysate with rabbit IgG antiserum to human MPO. The resulting precipitate from HL-60 blasts gave a major band of radioactivity of approximately 77,000 daltons and another band at approximately 46,000 daltons on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The MPO identity of the labeled bands was confirmed by cold competition. The relative mRNA activity expressed as a percentage of radioactivity incorporated into MPO (77,000-dalton band) as compared with total trichloracetic acid (TCA) precipitable radioactivity was 0.2%. Negligible mRNA activity for MPO was present in HL-60 granulocytes, HL-60 macrophages, and normal human granulocytes. Pulse- chase experiments showed that MPO was an approximate 75,000-dalton major band and 77,000-dalton minor band of radioactivity after HL-60 blasts were labeled for 1/2 hour with 35S-methionine and the cell lysate immunoprecipitated and subjected to SDS-PAGE. The chase experiments (one to 24 hours) showed that the 77,000- and 75,000-dalton bands of radioactivity were replaced with two major bands (55,000 and 15,000 daltons) and one minor band (approximately 39,000 daltons) of radioactivity. Six-hour 35S-methionine labeling experiments showed that the relative rate of MPO synthesis compared with total TCA precipitable radioactivity was 0.5% in HL-60 blasts and almost negligible in HL-60 macrophages and granulocytes, normal human granulocytes, and B- lymphocytes. The KG-1 myeloblasts and KG-1a early myeloblasts synthesized a small amount of the 75,000-dalton MPO protein. Although HL-60 cells no longer synthesized MPO after differentiation, HL-60 granulocytes and HL-60 macrophages continued to contain MPO as measured by enzyme activity.(ABSTRACT TRUNCATED AT 400 WORDS)

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Myeloperoxidase: its structure and expression during myeloid differentiation

Blood ◽

10.1182/blood.v65.2.484.bloodjournal652484 ◽

1985 ◽

Vol 65 (2) ◽

pp. 484-491 ◽

Cited By ~ 2

Author(s):

HP Koeffler ◽

J Ranyard ◽

M Pertcheck

Keyword(s):

Relative Rate ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Major Protein ◽

Trichloracetic Acid ◽

Major Band ◽

Minor Band ◽

Sds Page ◽

Human Granulocytes ◽

Normal Human

Myeloperoxidase (MPO) is a major protein present in myeloid cells and is used by these cells to help kill microbes. The human promyelocytic HL-60 line can be induced to differentiate to granulocytes or macrophagelike cells. Poly (A) containing RNA was isolated from HL-60 granulocytes, HL-60 macrophages, HL-60 blasts, and normal human granulocytes. The mRNA was translated in a reticulocyte lysate system in the presence of 35S-methionine. The MPO was precipitated from the lysate with rabbit IgG antiserum to human MPO. The resulting precipitate from HL-60 blasts gave a major band of radioactivity of approximately 77,000 daltons and another band at approximately 46,000 daltons on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The MPO identity of the labeled bands was confirmed by cold competition. The relative mRNA activity expressed as a percentage of radioactivity incorporated into MPO (77,000-dalton band) as compared with total trichloracetic acid (TCA) precipitable radioactivity was 0.2%. Negligible mRNA activity for MPO was present in HL-60 granulocytes, HL-60 macrophages, and normal human granulocytes. Pulse- chase experiments showed that MPO was an approximate 75,000-dalton major band and 77,000-dalton minor band of radioactivity after HL-60 blasts were labeled for 1/2 hour with 35S-methionine and the cell lysate immunoprecipitated and subjected to SDS-PAGE. The chase experiments (one to 24 hours) showed that the 77,000- and 75,000-dalton bands of radioactivity were replaced with two major bands (55,000 and 15,000 daltons) and one minor band (approximately 39,000 daltons) of radioactivity. Six-hour 35S-methionine labeling experiments showed that the relative rate of MPO synthesis compared with total TCA precipitable radioactivity was 0.5% in HL-60 blasts and almost negligible in HL-60 macrophages and granulocytes, normal human granulocytes, and B- lymphocytes. The KG-1 myeloblasts and KG-1a early myeloblasts synthesized a small amount of the 75,000-dalton MPO protein. Although HL-60 cells no longer synthesized MPO after differentiation, HL-60 granulocytes and HL-60 macrophages continued to contain MPO as measured by enzyme activity.(ABSTRACT TRUNCATED AT 400 WORDS)

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Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646313 ◽

1992 ◽

Vol 68 (05) ◽

pp. 534-538 ◽

Cited By ~ 5

Author(s):

Nobuhiko Yoshida ◽

Shingi Imaoka ◽

Hajime Hirata ◽

Michio Matsuda ◽

Shinji Asakura

Keyword(s):

Molecular Weight ◽

Sodium Dodecyl Sulfate ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Tetraacetic Acid ◽

Fibrin Monomer ◽

Sds Page ◽

Thrombotic Tendency ◽

Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

YARSI Medical Journal ◽

10.33476/jky.v26i2.394 ◽

2018 ◽

Vol 26 (2) ◽

pp. 058

Author(s):

Anna P. Roswiem ◽

Triayu Septiani

Keyword(s):

Sodium Dodecyl Sulphate ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Polyacrylamide Gel ◽

Sds Page

Bahan baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.

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Majra Honey Abrogated the Normal and Cancer Cells Proliferation Inhibition by Juniperus procera Extract and Extract/Honey Generated AgNPs

Anti-Cancer Agents in Medicinal Chemistry ◽

10.2174/1871520620666200213104224 ◽

2020 ◽

Vol 20 (8) ◽

pp. 970-981

Author(s):

Hamed A. Ghramh ◽

Essam H. Ibrahim ◽

Mona Kilnay

Keyword(s):

Anticancer Activity ◽

Cancer Cells ◽

Biological Activities ◽

Sugar Content ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Bioactive Molecules ◽

Sds Page ◽

Splenic Cells ◽

Juniperus Procera

Background: Juniperus procera and Majra honey are well-known as a folk medicine in many countries. Objectives: This work aimed to study the immunomodulatory effects after mixing Majra honey, J. procera water leaves extract and silver Nanoparticles (AgNPs) on immune or cancer cells. Methods: Juniperus procera water leaves extract and 20% Majra honey were prepared. Both the extract and honey were used separately to synthesize AgNPs. AgNPs were characterized using UV/Vis spectrophotometry and electron microscopy. Bioactive molecules in honey and the extract were explored using Fourier Transform Infrared (FT-IR) spectroscopy. Protein profile of honey was explored using Sodium Dodecyl Sulfate- Polyacrylamide Gel Electrophoresis (SDS-PAGE) and honey sugar content was determined using High- Performance Liquid Chromatography (HPLC). Biological activities of honey and the extract were tested. Results: The results demonstrated the ability of the extract/honey to produce AgNPs in a spherical shape. The extract/honey contained many functional groups. SDS-PAGE of Majra honey showed many protein bands. HPLC revealed honey is of good quality and no external additives are added to it. The extract and extract+ AgNPs inhibited the growth of normal rat splenic cells while honey stimulated it. The extract+honey turned stimulatory to the splenic cells’ growth and significantly diminished the inhibitory potential of the extract containing AgNPs. Both the extract and honey have antimicrobial activities, this potential increased in the presence of AgNPs. Honey and Honey+AgNPs inhibited HepG2 cancer cell proliferation while Hela cell growth inhibited only with honey+AgNPs. Conclusion: Both honey and the extract have antibacterial and immunomodulatory potentials as well as the power to produce AgNPs. Majra honey alone showed anticancer activity against HepGe2 cells, but not against Hela cells, and when contained AgNPs had anticancer activity on both cell lines. Mixing of Majra honey with J. procera extract showed characterized immunomodulatory potentials that can be described as immunostimulant.

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Study on cocoonase, sericin, and degumming of silk cocoon: computational and experimental

Journal of Genetic Engineering and Biotechnology ◽

10.1186/s43141-021-00125-2 ◽

2021 ◽

Vol 19 (1) ◽

Author(s):

Preeti Anand ◽

Jay Prakash Pandey ◽

Dev Mani Pandey

Keyword(s):

San Francisco ◽

Tertiary Structure ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Evolutionary Genetics ◽

Imaging Analysis ◽

Silk Cocoon ◽

Natural Color ◽

Sds Page

Abstract Background Cocoonase is a proteolytic enzyme that helps in dissolving the silk cocoon shell and exit of silk moth. Chemicals like anhydrous Na2CO3, Marseille soap, soda, ethylene diamine and tartaric acid-based degumming of silk cocoon shell have been in practice. During this process, solubility of sericin protein increased resulting in the release of sericin from the fibroin protein of the silk. However, this process diminishes natural color and softness of the silk. Cocoonase enzyme digests the sericin protein of silk at the anterior portion of the cocoon without disturbing the silk fibroin. However, no thorough characterization of cocoonase and sericin protein as well as imaging analysis of chemical- and enzyme-treated silk sheets has been carried out so far. Therefore, present study aimed for detailed characterization of cocoonase and sericin proteins, phylogenetic analysis, secondary and tertiary structure prediction, and computational validation as well as their interaction with other proteins. Further, identification of tasar silkworm (Antheraea mylitta) pupa stage for cocoonase collection, its purification and effect on silk sheet degumming, scanning electron microscope (SEM)-based comparison of chemical- and enzyme-treated cocoon sheets, and its optical coherence tomography (OCT)-based imaging analysis have been investigated. Various computational tools like Molecular Evolutionary Genetics Analysis (MEGA) X and Figtree, Iterative Threading Assembly Refinement (I-TASSER), self-optimized predicted method with alignment (SOPMA), PROCHECK, University of California, San Francisco (UCSF) Chimera, and Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) were used for characterization of cocoonase and sericin proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), protein purification using Sephadex G 25-column, degumming of cocoon sheet using cocoonase enzyme and chemical Na2CO3, and SEM and OCT analysis of degummed cocoon sheet were performed. Results Predicted 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. Na2CO3 treatment showed more degumming effect (i.e., cocoon sheet weight loss) as compared to degumming with cocoonase. However, cocoonase-treated silk cocoon sheet holds the natural color of tasar silk, smoothness, and luster compared with the cocoon sheet treated with Na2CO3. SEM-based analysis showed the noticeable variation on the surface of silk fiber treated with cocoonase and Na2CO3. OCT analysis also exemplified the variations in the cross-sectional view of the cocoonase and Na2CO3-treated silk sheets. Conclusions Present study enlightens on the detailed characteristics of cocoonase and sericin proteins, comparative degumming activity, and image analysis of cocoonase enzyme and Na2CO3 chemical-treated silk sheets. Obtained findings illustrated about use of cocoonase enzyme in the degumming of silk cocoon at larger scale that will be a boon to the silk industry.

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