scholarly journals Extraction and characterization of type 1 collagen from the skin and scales of Heterotis niloticus and Lates niloticus

2021 ◽  
Vol 1 (2) ◽  
pp. 01-10
Author(s):  
Victoria Ifeoluwa Ayo ◽  
Dickson Achimugu Musa ◽  
Evans Chidi Egwim
Keyword(s):  
Acetic Acid ◽  
Fish Species ◽  
Good Alternative ◽  
Extraction Process ◽  
High Quality ◽  
Alternative Source ◽  
Sds Page ◽  
Lates Niloticus

The study is aimed to extract and characterize collagens from the skin and scale of two selected Nigerian freshwater fish species (Heterotis niloticus and Lates niloticus) using either pepsin (PSC) or acid-soluble (ASC) extraction. The collagen was extracted using 0.5M acetic acid and pepsin. The collagen yield was determined and characterized by SDS PAGE, and FTIR. Collagen extraction yields varied with the extraction process; the yield was significantly higher in the skin (5.08±0.34–33.97±1.78 %) than in the scale (1.76–8.05 %). The absorption peaks of the extracted collagen using acetic acid and pepsin show that only ASC of skin (3344.27 cm-1) and scale (3495.85 cm-1) of H. niloticus shows the peaks characteristic of Amide A, while Amide B peaks of collagen extracted from the skin and scale of H. niloticus and L. niloticus were found at 2974.46 cm-1 and 2925.7 cm-1 , representing an asymmetrical stretch of CH2. Similarly, ASC on the skin (1558.36 cm-1) and scale (1576.46 cm-1) of H. niloticus shows the absorption peak characteristics of amide II. ASC on the skin of H. niloticus (1671.05 cm-1), PSC on scale of H. niloticus (1658.55 cm-1), and on scale of H. niloticus (1678.65 cm1) shows absorption peaks in range characteristic of amide 1. There were no differences in the skin and scale collagen profiles among the two fish species when characterized by SDS-PAGE. Our data revealed that the skin and scale of Lates niloticus and Heterotis niloticus could be a good alternative source of high-quality collagen for industries.

Extraction and Partial Characterization of Pepsin-Soluble Collagens from the Skin of Amiurus Nebulosus

2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
Skin Collagen ◽  
Maximal Yield ◽  
Pepsin Soluble Collagen

Pepsin-soluble collagen (PSC) was successfully extracted from the skin of Amiurus nebulosus. The skin of Amiurus nebulosus was immersed in 0.3 mol/L acetic acid (1: 20, m: V) for 6 h at 37°C, while pepsin was added, at a level of 5000U/g dosage of defatted skin. The maximal yield of the collagen was 97.44%, which was higher than that of acid-soluble collagen (ASC) at 62.05%. Some properties of pepsin-soluble collagens from the skin of Amiurus nebulosus were characterized. Amino acid composition and SDS-PAGE suggested that the collagen might be classified as type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements in PSC of Amiurus nebulosus skin of collagen. There is a possibility to use Amiurus nebulosus skin collagen as an alternative source of collagen for industrial purposes and subsequently it may maximize the economical value of the fish.

scholarly journals Partial purification and characterization of a type 1 protein phosphatase in purified nuclei of pea plumules

1996 ◽  
Vol 319 (3) ◽  
pp. 985-991 ◽  
Author(s):  
Yan-Lin GUO ◽  
Stanley J ROUX
Keyword(s):  
Protein Phosphatase ◽  
Specific Activity ◽  
Partial Purification ◽  
Rabbit Muscle ◽  
Phosphatase Inhibitors ◽  
Isolation And Characterization ◽  
Endogenous Protein ◽  
Sds Page

We report the isolation and characterization of a protein Ser/Thr phosphatase from highly purified pea nuclei. In subnuclear fractions, more than 75% of Ser/Thr protein phosphatase activity was associated with the chromatin fraction, whereas the other 25% was in the nuclear membrane/nucleoplasmic fraction when phosphorylase a was used as a substrate. The enzyme was purified approx. 2750-fold to a specific activity of approx. 4000 nmol/min per mg. The molecular mass of the enzyme was 34 kDa as estimated by molecular sieve chromatography, and approx. 40 kDa as estimated by SDS/PAGE. The phosphatase was inhibited by okadaic acid with an IC50 of approx. 15 nM, by rabbit muscle inhibitor 2 with an IC50 of approx. 10 nM, and by microcystin-LR with an IC50 of approx. 0.05 nM. The enzyme did not require Ca2+, Mg2+ or Mn2+ for its activity; instead, these cations showed some inhibitory effects. It was inhibited by NaF or citrate but not by tartrate, molybdate or vanadate under the conditions tested. Its sensitivities towards the various phosphatase inhibitors and its substrate specificity were very similar to those characteristic of the type 1 Ser/Thr protein phosphatases well studied in animal systems. The enzyme was able to selectively dephosphorylate a 92 kDa nuclear protein that had been phosphorylated by one or more endogenous protein kinases.

scholarly journals Euthynnus affinis viscera-an alternative source for protease and lipase enzymes: Characteristic and potential application as destainer agent

2020 ◽  
Vol 21 (12) ◽  
Author(s):  
Vivi Mardina ◽  
Tisna Harmawan ◽  
Fitriani Fitriani ◽  
ELLY SUFRIADI ◽  
Febriani Febriani ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Palm Oil ◽  
Potential Application ◽  
Partial Purification ◽  
Alkaline Ph ◽  
Ammonium Sulfate Precipitation ◽  
Alternative Source ◽  
Sds Page ◽  
Euthynnus Affinis

Abstract. Mardina V, Harmawan T, Fitriani, Sufriadi E, Febriani, Yusof F. 2020. Euthynnus affinis viscera-an alternative source for protease and lipase enzymes: Characteristic and potential application as destainer agent. Biodiversitas 21: 5858-5864. This study described the characterization of protease and lipase, extracted from the viscera of Euthynnus affinis and their applications as stains removal. Enzyme increased a few folds (3.99 folds for protease and 2.45 folds for lipase) after the submission to partial purification processes by ammonium sulfate precipitation and dialysis. Molecular mass assessment by SDS-PAGE showed that the enzyme solution contains three protein bands, estimated at 70, 42, and 24 kDa for protease and 32 kDa for lipase. Zymography confirmed the presence of protease and lipase in the sample. The protease and lipase exhibited optimum activities at pH 7.0 and pH 8.0 respectively, active at temperatures from 35 to 75oC with optimal activities at 65oC for both. The enzymes were stable at alkaline pH after 90 minutes (mins) of incubation and were also stable up to 65oC, showing the remaining activities of more than 70%. Samples containing protease and lipase as de-staining agents were tested by their ability to remove blood and palm oil stains, with results proving they were effective. Overall, the study showed that crude fish visceral extract contains protease and lipase and is useful in removing household stains, and could substitute for commercial detergents.

scholarly journals Identification of Active Compounds of Annona muricata (Soursop) Leaf Wax Extract Using GC-MS

2020 ◽  
pp. 17-21
Author(s):  
Fai F. Yirankinyuki ◽  
Buhari Magaji ◽  
Wilson L. Danbature ◽  
Abdullah M. Abdullah
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Good Alternative ◽  
Gas Chromatography Mass Spectrometry ◽  
Annona Muricata ◽  
Industrial Chemicals ◽  
Alternative Source ◽  
Active Compounds ◽  
Leaf Wax

Soursop plant (Annona muricata L.), is widely used for both industrial and medicinal applications. In view of this, the present study aims at extraction and characterization of soursop leaf wax using gas chromatography-mass spectrometry (GC-MS). The results of the GC-MS analysis of soursop wax show the presence of 26 different compounds. From the results, it could be concluded that A. muricata contains various compounds that could be useful in different industries. Thus, soursop wax could be a good alternative source for many industrial chemicals that are currently sourced from petroleum which is non-renewable.

scholarly journals Isolation and properties of collagen extracted from mixed by-products obtained from different fish species

Biotecnia ◽  
2021 ◽  
Vol 23 (3) ◽  
pp. 109-116
Author(s):  
Celia Olivia García-Sifuentes ◽  
Julio Cesar Zamorano-Apodaca ◽  
Marcel Martinez-Porchas ◽  
Susana Maria Scheuren-Acevedo ◽  
Miguel Angel Mazorra-Manzano
Keyword(s):  
Fish Species ◽  
Type I Collagen ◽  
Helical Structure ◽  
Extraction Process ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
By Products

Fish by-products consisting of skin, bones, or scales are collagen sources. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) mixed by-products derived from different fish species were extracted and evaluated. The properties evaluated for both collagens were chemical composition, amino acid- and SDS-PAGE- protein profiles, Fourier transform infrared spectroscopy (FTIR), denaturation temperature (Tmax), enthalpy (ΔH), and solubility. The ASC and PSC registered a protein content of 48.56 and 38.80 %, respectively. From the total amino acids detected, hydroxyproline accounted for 7 % and 6 % for ASC and PSC, respectively. The electrophoretic profile showed the presence of the type I collagen bands (α1, α2, β, and γ), whereas FTIR spectrum showed the presence of diverse collagen functional groups (Amide A, B, I, II, and III) for both extracted types, and demonstrated that the extraction process did not affect the collagen´s triple-helical structure. The Tmax of ASC and PSC were 38.27 and 38.07° C, respectively, whereas ΔH were 0.64 and 0.33 J g-1. The lowest solubility was registered at pH 5 for ASC and pH 9 for PSC. The caractheristics of the collagen extracted, indicated that a mixture of by-products from different species could be an alternative for their reutilization by the local markets.

436-P: Characterization of Autoimmunity in the Acceleration of Atherosclerosis in Type 1 Diabetes

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 436-P
Author(s):  
KYOUNGMIN PARK ◽  
QIAN LI ◽  
HYUNSEOK PARK ◽  
RONALD ST-LOUIS ◽  
JIALIN FU ◽  
...  
Keyword(s):  
Type 1 Diabetes

Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

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