1.Antibacterial activity of Bombyx mori and Samia cynthia ricini sericin proteins against Escherichia coli and Staphylococcus aureus
Lisa Aprilia ; Yuni Cahya Endrawati ; Irma Isnafia Arief
Malaysian Journal of Microbiology 2022;18(5):547-554
Aims:
This study was designed to investigate the antibacterial properties of the sericin protein Bombyx mori and Samia cynthia ricini against Gram-negative Escherichia coli and Gram-positive Staphylococcus aureus strains.
Methodology and results:
Sericin protein was extracted from the cocoons of B. mori races A, B, C, D, F1-1, F1-2 and S. ricini from Indonesia using a degumming process. The extracted sericin protein was evaluated as anti-microbials using Kirby Breuer disc diffusion, spectrometer measurement in decreasing OD value and imaging scanning electron microscope (SEM). The tests revealed that sericin protein from B. mori was more capable of inhibiting bacteria S. aureus than E. coli. Sericin protein from S. ricini was also capable of strongly inhibiting both S. aureus and E. coli bacteria. The sericin proteins of B. mori and S. ricini were found to reduce the number of S. aureus and E. coli bacteria as the OD value decreased at a concentration of 9%. The SEM imaging suggests that sericin B. mori and S. ricini proteins caused changes in cell morphology in S. aureus and E. coli bacteria, resulting in bacterial cell function disruption and death.
Conclusion, significance and impact of study
Bombyx mori and S. ricini sericin proteins were found to act against S. aureus and E. coli bacteria. Therefore, sericin protein has a greater antibacterial activity against Gram-positive strain S. aureus.
Anti-Bacterial Agents
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Sericins
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Bombyx
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Lepidoptera
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Escherichia coli
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Staphylococcus aureus
2.Analysis of protective mechanism of silk protein based cryoprotectants.
Xinli ZHOU ; Yukun DU ; Yun TENG ; Xiaomin ZHANG
Journal of Biomedical Engineering 2019;36(6):986-993
Dimethyl sulfoxide (Me SO) supplemented with fetal bovine serum (FBS) is a widely used cryoprotectant combination. However, high concentration of Me SO is toxic to cells, and FBS presents problems related to diseases such as bovine spongiform encephalopathy and viral infections. Silk protein is a kind of natural macromolecule fiber protein with good biocompatibility and hydrophilicity. The aim of this paper is to analyze the cryoprotective mechanism of silk protein as cryoprotectant. Firstly, differential scanning calorimetry (DSC) was used to measure the thermal hysteresis activity (THA) of silk protein. The THA of 10 mg/mL sericin protein was 0.96°C, and the THA of 10% (V/V) fibroin protein was 1.15°C. Then the ice recrystallization inhibition (IRI) of silk protein-PBS solution was observed with cryomicroscope. The cold stage was set at - 7°C, after 40 minutes' incubation, the mean grain size rate (MGSR) of sericin protein and fibroin protein were 28.99% and 3.18%, respectively, which were calculated relative to phosphate buffer saline (PBS) control. It is indicated that sericin and silk fibroin have certain effects of inhibiting recrystallization of ice crystals. Finally, the structure and physicochemical properties of silk protein were analyzed by Fourier transform infrared spectroscopy (FTIR). The results showed that the content of the random coil was 75.62% and the β-sheet structure was 24.38% in the secondary of sericin protein. The content of the β-sheet structure was 56.68%, followed by random coil structure 22.38%, and α-helix 16.84% in the secondary of fibroin protein. The above analysis demonstrates the feasibility of silk fibroin as a cryoprotectant, and provides a new idea for the selection of cryoprotectants in the future.
Animals
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Bombyx
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Calorimetry, Differential Scanning
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Fibroins
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Sericins
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Silk
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Spectroscopy, Fourier Transform Infrared
3.Sensitization to silk allergen among workers of silk filatures in India: a comparative study
Giriyanna GOWDA ; Anwith Huluvadi SHIVALINGAIAH ; Anagha Manakari VIJAYEENDRA ; Nivedita SARKAR ; Chitra NAGARAJ ; Nugehally Raju Ramesh MASTHI
Asia Pacific Allergy 2016;6(2):90-93
BACKGROUND: Sericulture plays an eminent role in development of rural economy in India. Silk filature is a unit where silk is unwound from the cocoons and the strands are collected into skeins. During the process workers are exposed to the high molecular weight proteins like Sericin and Fibroin which are potent allergens leading to sensitization over a period of time and subsequently occupational related health disorders. OBJECTIVE: To identify and compare the magnitude of silk allergen sensitization in workers of silk filatures. METHODS: A community based comparative descriptive study was conducted for a period of 1 year at Ramanagara in south India. One hundred twenty subjects working in the silk filatures formed the study group. For comparison, 2 types of controls were selected viz.120 subjects who were not working in the silk filatures but resided in the same geographical area (control A) and 360 subjects who were not working in silk filatures as well not residing in the same geographical area (control B). Skin prick test was used to identify the silk allergen sensitization. RESULTS: Mean age was 34.14 ± 2.84 years in the study group. Mean age was 40.59 ± 14.40 years and 38.54 ± 12.20 years in control A and control B, respectively. There were 35 males (29.16%) and 85 females (70.84%) in the study group. There were 58 (48.34%) males and 62 (51.66%) females and 152 (42.2%) males and 208 females (57.8%) in control A and control B, respectively. Sensitization to silk allergen was 35.83% in the study group and 20.83% in the control group A and 11.11% in control group B. There was difference in the allergen sensitivity between the study group and control groups and it was statistically significant (chi-square = 38.08; p < 0.001). CONCLUSION: There is high burden of silk allergen sensitization among silk filature workers.
Allergens
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Female
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Fibroins
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Humans
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India
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Male
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Molecular Weight
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Sericins
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Silk
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Skin
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Skin Tests
4.Dietary effect of silk protein on epidermal levels of free sphingoid bases and phosphate metabolites in NC/Nga mice.
Youngae KIM ; Eun hwa SONG ; Kyoungoh SHIN ; Yongmoon LEE ; Yunhi CHO
The Korean Journal of Nutrition 2012;45(2):113-120
In our previous studies, dietary supplements of silk protein, sericin, and fibroin, were beneficial for improving epidermal levels of ceramides, which are the major lipids for maintaining the epidermal barrier. In this study, we investigated the dietary effects of silk protein on epidermal levels of free sphingoid bases and their phosphates such as C18 sphingosine (So), C18 sphinganine (Sa), C18 sphingosine-1-phosphate (S1P), and C18 sphinganine-1-phosphate (Sa1P), which are either synthetic substrate or degradative metabolites of ceramides. Forty-five male NC/Nga mice, an animal model of atopic dermatitis (AD), were divided into three groups: group CA was an atopic control and fed a control diet, group S was fed a 1% sericin diet, and group F was fed a 1% fibroin diet. Fifteen male BALB/c mice served as group C (control group) and were fed the control diet. All mice were fed with diets and water ad libitum for 10 weeks. Sa in group CA was lower than that in group C, but So in group CA was similar to that in group C. So and Sa were higher in groups S and F than those in group CA; So level was even higher than that in group C, and Sa level was similar to that of group C. The So/Sa ratio in group CA, which is reported to increase in AD, was significantly higher than that of group C. The So/Sa ratio was lower in groups S and F than that in group CA, and decreased further in group F. However, S1P and Sa1P in groups S and F were similar to those in group CA. Taken together, we demonstrated that silk protein, sericin and fibroin dietary supplements, increased So and Sa levels, and decreased the So/Sa ratio.
Animals
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Ceramides
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Dermatitis, Atopic
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Diet
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Dietary Supplements
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Fibroins
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Humans
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Lysophospholipids
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Male
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Mice
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Models, Animal
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Phosphates
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Sericins
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Silk
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Sphingosine
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Water
5.Protective effect of sericin peptide against alcohol-induced gastric injury in mice.
You-gui LI ; Dong-feng JI ; Tian-bao LIN ; Shi ZHONG ; Gui-yan HU ; Shi CHEN
Chinese Medical Journal 2008;121(20):2083-2087
BACKGROUNDSericin peptide (SP) has shown a powerful anti-oxidant property in a host of studies. The present study was designed to investigate the possible protective effects of SP against alcohol-induced gastric lesions in mice and to explore the potential mechanisms.
METHODSAnimals were randomly divided into 5 groups: control, alcohol (56%, 14.2 ml/kg), SP-treated mice (0.2, 0.4, 0.8 g/kg). Mice were pretreated with SP before administering alcohol, the concentration of ethanol in serum and urine, the contents of malondialdehyde (MDA), glutathione (GSH) and the glutathione peroxidase (GSH-PX), catalase (CAT) and superoxide dismutase (SOD) activities in the gastric mucosa were measured, subsequently, the pathological evaluation of stomach was also observed.
RESULTSOf the animals pre-treated with SP (0.4, 0.8 g/kg), the concentration of ethanol in serum was significantly decreased, while increased in urine as compared to the alcohol-administered alone animals. Alcohol administration caused severe gastric damage as indicated by markedly increased MDA levels and decreased antioxidants, such as reduced GSH, GSH-PX and SOD in the gastric tissue while the CAT activity was not altered. On SP administration there was a reversal in these values towards normal. Histopathological studies confirmed the beneficial role of SP, which was in accordance with the biochemical parameters.
CONCLUSIONSSP could protect gastric mucosa from alcohol-induced mucosal injury. These gastroprotective effects might be due to increasing 'first-pass metabolism' in the stomach and hastening ethanol elimination directly through the urine. SP might also play an important role in the protection of the structure and function of gastric mitochondria, at least partly based on their anti-oxidant effect.
Amino Acids ; analysis ; Animals ; Cytoprotection ; Ethanol ; blood ; toxicity ; urine ; Gastric Mucosa ; drug effects ; pathology ; Glutathione ; metabolism ; Male ; Mice ; Mice, Inbred ICR ; Sericins ; analysis ; pharmacology ; Superoxide Dismutase ; metabolism
6.Preparation and cytocompatibility study of poly (epsilon-caprolactone)/silk sericin nanofibrous scaffolds.
Haibin LI ; Linhao LI ; Yuna QIAN ; Kaiyong CAI ; Yonggang LU ; Li ZHONG ; Wanqian LIU ; Li YANG
Journal of Biomedical Engineering 2011;28(2):305-309
Three-dimensional poly (epsilon-caprolactone)/silk sericin (PCL/SS) porous nanofibrous scaffolds were prepared by electrospinning. The structure and properties of the scaffolds were characterized by Scanning Electron Microscope (SEM), Transmission Electron Microscope (TEM), Fourier Transform Infrared Spectroscopy (FTIR) and water contact angle instrument. Studies on cell adhension and proliferation were carried out by culturing human primary skin fibroblast cells (FEK4) on these scaffolds using SEM and MTS. The experimental results showed that the PCL/SS nanofibrous scaffolds with SS nanoparticles had porous non-woven mesh structure with nanofibrous cross-linked with each other. Fiber diameter was very uniform and precise, and the secondary structure of SS protein had not been changed. Furthermore, the capability of hydrophile increased with the SS addition, which improved FEK4 cells adhesion and proliferation on the scaffolds.
Biocompatible Materials
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chemistry
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Cell Adhesion
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drug effects
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Cells, Cultured
;
Fibroblasts
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cytology
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Microscopy, Electron
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Nanofibers
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chemistry
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Polyesters
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chemistry
;
Sericins
;
chemistry
;
Silk
;
chemistry
;
Spectroscopy, Fourier Transform Infrared
;
Tissue Scaffolds
;
chemistry
7.Dietary Effect of Silk Protein Sericin or Fibroin on Plasma and Epidermal Amino Acid Concentration of NC/Nga Mice.
Hyunae KIM ; Kyung Ho PARK ; Joo Hong YEO ; Kwang Gill LEE ; Do Hyeon JEONG ; Sung Han KIM ; Yunhi CHO
The Korean Journal of Nutrition 2006;39(6):520-528
Free amino acids in epidermis function as a major component of Natural Moisturizing Factor (NMF), which maintains the optimal level of water in skin even at the low humidity. In fact, the depletion of free amino acids is reported in the epidermis of atopic dermatitis, the skin condition involving dryness. As an effort searching the dietary source for improving the level of water and free amino acid in epidermis, the dietary effects of silk protein, sericin (S) and fibroin (F) on trans epidermal water loss (TEWL), and plasma and epidermal levels of free amino acids were compared in this study. Thirty of male NC/Nga mice, an animal model of atopic dermatitis, were divided into three groups: group CA as an atopic control with control diet, group S: 1% sericin diet and group F: 1% fibroin diet. Ten of male BALB/c mice were served as group C (control group) with control diet. All mice were fed on diet and water ad libitum for 10weeks. Dry skin condition was established in group CA as TEWL was increased (148.7% of group C). In parallel, epidermal level of glutamate, one of major amino acids functioning as NMF, was dramatically decreased and epidermal levels of methionine and alanine were inversely elevated. Dietary supplementation of sericin (group S) reduced TEWL at the similar level with group C and increased epidermal levels of glutamate as well as serine and glycine, the other major amino acids as NMF. Despite a marked decrease of methionine and alanine, the reduction of TEWL and epidermal levels of glutamate, serine and glycine of group F were less than of group S. Furthermore, in contrast to similar levels of other free amino acids in plasma and epidermis of group S and group C, plasma and epidermal levels of other free amino acids, specifically phenylalanine, isoleucine, cysteine and tyrosine in epidermis of group F, were significantly higher than of group C. Together, our data demonstrate that dietary supplementation of sericin is more effective at improving dry skin condition that paralleled with the normalization of free amino acids in plasma and epidermis of NC/Nga mice.
Alanine
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Amino Acids
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Animals
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Cysteine
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Dermatitis, Atopic
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Diet
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Dietary Supplements
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Epidermis
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Fibroins*
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Glutamic Acid
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Glycine
;
Humans
;
Humidity
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Isoleucine
;
Male
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Methionine
;
Mice*
;
Models, Animal
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Phenylalanine
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Plasma*
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Sericins*
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Serine
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Silk*
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Skin
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Tyrosine