scholarly journals Pangasius Fish Skin and Swim Bladder as Gelatin Sources for Hard Capsule Material

2021 ◽  
Vol 2021 ◽  
pp. 1-6
Author(s):  
Mala Nurilmala ◽  
Noviyan Darmawan ◽  
Erin Apriliani Wulandari Putri ◽  
Agoes M. Jacoeb ◽  
Tun Tedja Irawadi
Keyword(s):  
Water Content ◽  
Base Material ◽  
Gel Strength ◽  
Swim Bladder ◽  
Fish Skin ◽  
Disintegration Time ◽  
Sds Page ◽  
Capsule Material

In this paper, we report the extraction and characterization of gelatin from the abundant industrial fishery waste of Pangasius skin and swim bladder and its application as the base material for hard capsule shells. The yield of gelatin ranged between 19 and 23%, content of moisture is 7.6–9.2%, ash is 1.1–1.7%, pH is 4.1–5.2, gel strength is 238–278 bloom, and viscosity is 65–74.7% mP. SDS-PAGE showed all gelatins have chains of α1, α2, and β-peptides. The skin, swim bladder, and mixed gelatins were successfully used in the production of hard capsule shells. The dimensions, weight, disintegration time, and water content properties of the hard capsules from these Pangasius wastes were akin to the standards of commercial capsules.

scholarly journals Quality of Cultured Wader Pari During Storage at Different Temperature

2017 ◽  
Vol 20 (2) ◽  
pp. 339 ◽  
Author(s):  
Mala Nurilmala ◽  
Agoes Mardiono Jacoeb ◽  
Rofi Ahmad Dzaky
Keyword(s):  
Molecular Weight ◽  
Functional Group ◽  
Gel Strength ◽  
Yellowfin Tuna ◽  
Fish Skin ◽  
Alternative Source ◽  
Food Industries ◽  
Sds Page ◽  
Fish Skin Gelatin

Gelatin is one of the products which become a necessity for various industries, i.e. food and non-food industries. The application of gelatin has been increasing year by year in Indonesia. However, there is no<br />gelatin industry in Indonesia so far. Thus, it is necessary to find an alternative source of gelatin, especially from fishery by products.Thus, the purpose of this research was to extract fish skin gelatin of yellowfin tuna with temperature treatments (55, 65 and 75oC). In addition, the properties of resulted gelatin were determined including yield, pH, gel strength, viscosity, functional groups, molecular weight profiles, and amino acid composition. The extraction at 75oC was chosen as the best result. The yield was 17%; pH 5.3; gel strength 1789.55 gf, viscosity 104.2 Cp, respectively. There was functional group amide A, I, II, dan III. SDS-PAGE showed β, α1 dan α2 bands for tuna skin gelatin. In addition, the main amino acids were glycine and proline.

scholarly journals The Effect of Gelatin from Different Fish Skin on Physical and Sensory Characteristics of Marsmallow

2019 ◽  
Vol 21 (1) ◽  
pp. 17
Author(s):  
Izmy Nur Aziza ◽  
Yudhomenggolo Sastro Darmanto ◽  
Retno Ayu Kurniasih
Keyword(s):  
Water Content ◽  
Gel Strength ◽  
Partial Hydrolysis ◽  
Fish Skin ◽  
Parametric Data ◽  
Randomized Design ◽  
Honestly Significant Difference ◽  
Significant Difference ◽  
Fish Skin Gelatin

Gelatin is one type of protein obtained from partial hydrolysis of natural collagen. Utilization of gelatin has been widely applied to food, especially in foods related to elastic texture, for example marshmallow. The purpose of this research was to determine the quality of various types of gelatin based on gel strength, elsticity, water content, hedonic and to know the best marshmallow. The experimental design was complete randomized design. The treatment was different fish skin gelatin, namely patin, payus, and cobia with concentration of 7.39%. The parameters consisted of gelatin tests (yield, gel strength, viscosity) and marshmallow tests (gel strength, elasticity, water content and hedonic). Parametric data were analyzed with Analysis of Varience test and continued with Honestly Significant Difference test. The results showed that the use of different skin had significantly different (P<0.05) on yield, gel strength and viscosity, with the result of patin (13.24%, 280.56 bloom, 2.05 cP), payus (15.47%, 328 bloom, 3.18 cP), cobia 17.88%, 392.24 bloom, 5.63, respectively. The use of gelatin from payus and cobia had significantly different (P<0.05) to marshmallow characteristic. Marshmallow with gelatin skin of cobia fish had gel strength 1564.19 g.cm, elasticity 95.16 mm, water content 14.41% and hedonic test with interval of of 7.52 < μ < 7.91 which was means liked by panelists.

Effects of Hydrochloric Acid Concentration on the Properties of Black Tilapia Fish Skin Gelatin

2016 ◽  
Vol 840 ◽  
pp. 165-169 ◽  
Author(s):  
Norhasikin Ismail ◽  
Hasan Zuhudi Abdullah
Keyword(s):  
Hydrochloric Acid ◽  
Acid Concentration ◽  
Storage Time ◽  
Gel Strength ◽  
Hydrochloric Acid Concentration ◽  
Fish Skin ◽  
Percentage Yield ◽  
Fish Skin Gelatin ◽  
Pre Treatment

Gelatin extractedfrom fish skin is an alternativeresource instead of mammalian animals. Theextraction process of gelatin from black tilapia skin was carried out throughthe use of hydrochloric acid (HCl) with different concentration (0.05 M – 1.0 M)and followed by a final extraction with water at 50°C for 4 hours and endedwith drying. Characterization of gel strength was done in accordance with BSI:1975while moisture content and percentage yield on wet basis with AOAC 1999. Theeffects of acid concentration used during pre-treatment process on yield andphysical properties of fish gelatin were measured. The yield of gelatin for0.05 M and 1.0 M were 10.45% to 22.25% respectively. The gel strength ofgelatin at 0.05 M is the highest (833 g) due to longer storage time. Gelatin whichtreated with high acid concentration gives lower in gel strength that suitableas an edible gelatin.

Characterization of frozen hydrated biological specimens by low-loss EELS

1992 ◽  
Vol 50 (2) ◽  
pp. 1572-1573
Author(s):  
Songquan Sun ◽  
Richard D. Leapman
Keyword(s):  
Water Content ◽  
Direct Method ◽  
Internal Standard ◽  
Dry Weight ◽  
Dark Field ◽  
Protein Solutions ◽  
Subcellular Compartment ◽  
Differential Shrinkage ◽  
Electron Energy Loss

Analyses of ultrathin cryosections are generally performed after freeze-drying because the presence of water renders the specimens highly susceptible to radiation damage. The water content of a subcellular compartment is an important quantity that must be known, for example, to convert the dry weight concentrations of ions to the physiologically more relevant molar concentrations. Water content can be determined indirectly from dark-field mass measurements provided that there is no differential shrinkage between compartments and that there exists a suitable internal standard. The potential advantage of a more direct method for measuring water has led us to explore the use of electron energy loss spectroscopy (EELS) for characterizing biological specimens in their frozen hydrated state.We have obtained preliminary EELS measurements from pure amorphous ice and from cryosectioned frozen protein solutions. The specimens were cryotransfered into a VG-HB501 field-emission STEM equipped with a 666 Gatan parallel-detection spectrometer and analyzed at approximately −160 C.

KARAKTERISTIK ABON IKAN GABUS (Channa striata) DENGAN SUBTITUSI KLUWIH (Artocarpus camansi)

2018 ◽  
Vol 16 (2) ◽  
pp. 219-226
Author(s):  
Sri Rizqi Annisa ◽  
Dewi Larasati ◽  
Endang Bekti K
Keyword(s):  
Protein Content ◽  
Water Content ◽  
Analysis Of Variance ◽  
Fiber Content ◽  
Substitution Treatment ◽  
Fish Fillet ◽  
Organoleptic Test ◽  
Average Water ◽  
Channa Striata

The aim of this study was to determine the characterization of shredded mureel fish with kluwih substitution on water content, protein content, fiber content and organoleptic (preference for crispness and taste). This study uses a simple Randomized Complete Design (RCD) with the substitution treatment of kluwih and mureel fish, with the following ratio: S1 (240g: 60g), S2 (210g: 90g), S3 (180g: 120g), S4 (150g: 150g), S5 (120g: 180g). Data were analyzed statistically by analysis of variance and if there was a significant effect, further testing was done with BNJ at the level of 5%. The results showed that kluwih substitution in the manufacture of mureel fish shredded had an average: water content of 8.33-10.62%, protein :16.83-22.00%, fiber : 6.79-6.99%, score crispness 2-6.12, taste score 2.6-6.6. Based on the results of the analysis of the variety of kluwih substitutes and mureel fish have a significant effect on water content, protein content and crisp organoleptic test, taste on mureel fish fillet, and no significant effect on fiber content. The best kluwih substitution in S3 treatment with 120 grams of substitute kluwih and 180 grams of mureel fish.

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.

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

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

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.

scholarly journals Identification and characterization of Sulfolobus solfataricusD-gluconate dehydratase: a key enzyme in the non-phosphorylated Entner–Doudoroff pathway

2005 ◽  
Vol 387 (1) ◽  
pp. 271-280 ◽  
Author(s):  
Seonghun KIM ◽  
Sun Bok LEE
Keyword(s):  
Molecular Mass ◽  
Gel Filtration ◽  
Maximal Activity ◽  
Genome Database ◽  
Sds Page ◽  
Key Enzyme ◽  
Bivalent Metal Ions ◽  
Ammonium Sulphate Fractionation ◽  
Identification And Characterization

The extremely thermoacidophilic archaeon Sulfolobus solfataricus utilizes D-glucose as a sole carbon and energy source through the non-phosphorylated Entner–Doudoroff pathway. It has been suggested that this micro-organism metabolizes D-gluconate, the oxidized form of D-glucose, to pyruvate and D-glyceraldehyde by using two unique enzymes, D-gluconate dehydratase and 2-keto-3-deoxy-D-gluconate aldolase. In the present study, we report the purification and characterization of D-gluconate dehydratase from S. solfataricus, which catalyses the conversion of D-gluconate into 2-keto-3-deoxy-D-gluconate. D-Gluconate dehydratase was purified 400-fold from extracts of S. solfataricus by ammonium sulphate fractionation and chromatography on DEAE-Sepharose, Q-Sepharose, phenyl-Sepharose and Mono Q. The native protein showed a molecular mass of 350 kDa by gel filtration, whereas SDS/PAGE analysis provided a molecular mass of 44 kDa, indicating that D-gluconate dehydratase is an octameric protein. The enzyme showed maximal activity at temperatures between 80 and 90 °C and pH values between 6.5 and 7.5, and a half-life of 40 min at 100 °C. Bivalent metal ions such as Co2+, Mg2+, Mn2+ and Ni2+ activated, whereas EDTA inhibited the enzyme. A metal analysis of the purified protein revealed the presence of one Co2+ ion per enzyme monomer. Of the 22 aldonic acids tested, only D-gluconate served as a substrate, with Km=0.45 mM and Vmax=0.15 unit/mg of enzyme. From N-terminal sequences of the purified enzyme, it was found that the gene product of SSO3198 in the S. solfataricus genome database corresponded to D-gluconate dehydratase (gnaD). We also found that the D-gluconate dehydratase of S. solfataricus is a phosphoprotein and that its catalytic activity is regulated by a phosphorylation–dephosphorylation mechanism. This is the first report on biochemical and genetic characterization of D-gluconate dehydratase involved in the non-phosphorylated Entner–Doudoroff pathway.

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