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Special Issue "Gelatin: Chemistry, Characterization, Application"

A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: 30 November 2018

Special Issue Editor

Guest Editor
Dr. Silvia Panzavolta

Alma Mater Studiorum Universita di Bologna, Department of Chemistry "G. Ciamician", Bologna, Italy
Website | E-Mail
Interests: biopolymers; biomimetic materials; calcium phosphate bone cement; drug delivery systems; gelatin scaffolds for osteochondral tissue engineering

Special Issue Information

Dear Colleagues,

This Special Issue is related to the chemistry, characterization and application of gelatin. Gelatin, obtained by chemical-thermal degradation of collagen, is one of the most employed biopolymers, thanks to its biodegradability, excellent biocompatibility, plasticity, adhesiveness, abundance, and low cost. The main drawbacks of gelatin as a material are its poor mechanical performance and its high solubility in aqueous environments, which can be improved through crosslinking or by combining the biopolymer with an inorganic filler. Gelatin-based materials could be developed and applied in multidisciplinary fields, for example packaging, food, pharmaceutical industry, cosmetic industry, as well as for the production of materials addressed to biomedical field.

All researchers working in the field are cordially invited to contribute original research papers or reviews to this Special Issue of Molecules, which focuses on gelatin new crosslinking methods, on the design and synthesis of gelatin-based biomaterials and scaffolds for osteochondral defect repair, on the performance of gelatin as tailored drug delivery systems, on the evaluation of novel gelatin-based materials for cosmetic and packaging applications, as well as on the characterization of chemical-physical properties with advanced analyses.

Dr. Silvia Panzavolta
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Gelatin crosslinking
  • Gelatin-based biomaterials
  • Gelatin as delivery system of bioactive molecules
  • Gelatin films and patches
  • Gelatin characterization

Published Papers (2 papers)

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Research

Open AccessArticle The Growth Proliferation, Apoptotic Prevention, and Differentiation Induction of the Gelatin Hydrolysates from Three Sources to Human Fetal Osteoblasts (hFOB 1.19 Cells)
Molecules 2018, 23(6), 1287; https://doi.org/10.3390/molecules23061287 (registering DOI)
Received: 1 April 2018 / Revised: 26 April 2018 / Accepted: 8 May 2018 / Published: 28 May 2018
PDF Full-text (20893 KB) | HTML Full-text | XML Full-text
Abstract
Gelatins from the skin of bovine, porcine, and tilapia were hydrolyzed to three degrees of hydrolysis (DH) by alcalase, neutrase, and papain, respectively. These hydrolysates at 0.02–0.1 g/L promoted the growth of human fetal osteoblasts by 101.4–135.7%, while higher DH or using papain
[...] Read more.
Gelatins from the skin of bovine, porcine, and tilapia were hydrolyzed to three degrees of hydrolysis (DH) by alcalase, neutrase, and papain, respectively. These hydrolysates at 0.02–0.1 g/L promoted the growth of human fetal osteoblasts by 101.4–135.7%, while higher DH or using papain and tilapia gelatins resulted in higher proliferation. The hydrolysates from porcine and tilapia gelatins at 0.05 g/L prevented induced apoptosis (decreasing total apoptotic proportions from 28.4% or 35.2% to 10.3–17.5% or 16.0–23.6%), and had differentiation induction (increasing alkaline phosphatase activity by 126.9–246.7% in early differentiation stage, or enhancing osteocalcin production by 4.1–22.5% in later differentiation stage). These hydrolysates had a similar amino acid profile; however, tilapia gelatin hydrolysates by papain with DH 15.4% mostly displayed higher activity than others. Tilapia gelatin hydrolysate could up-regulate β-catenin, Wnt 3a, Wnt 10b, cyclin D1, and c-Myc expression at mRNA levels by 1.11–3.60 folds, but down-regulate GSK 3β expression by 0.98 fold. Of note, β-catenin in total cellular and nuclear protein was up-regulated by 1.14–1.16 folds but unchanged in cytoplasmic protein, Wnt 10b, cyclin D1, and c-Myc expression were up-regulated by 1.27–1.95 folds, whilst GSK 3β expression was down-regulated by 0.87 fold. Activation of Wnt/β-catenin pathway is suggested to mediate cell proliferation and differentiation. Full article
(This article belongs to the Special Issue Gelatin: Chemistry, Characterization, Application)
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Open AccessArticle On-Demand Microwave-Assisted Fabrication of Gelatin Foams
Molecules 2018, 23(5), 1121; https://doi.org/10.3390/molecules23051121
Received: 5 April 2018 / Revised: 1 May 2018 / Accepted: 2 May 2018 / Published: 9 May 2018
PDF Full-text (2171 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Ultraporous gelatin foams (porosity >94%, ρ ≈ 0.039–0.056 g/cm3) have been fabricated via microwave radiation. The resulting foam structures are unique with regard to pore morphology (i.e., closed-cell) and exhibit 100% macroporosity (pore size 332 to 1700 μm), presence of an
[...] Read more.
Ultraporous gelatin foams (porosity >94%, ρ ≈ 0.039–0.056 g/cm3) have been fabricated via microwave radiation. The resulting foam structures are unique with regard to pore morphology (i.e., closed-cell) and exhibit 100% macroporosity (pore size 332 to 1700 μm), presence of an external skin, and densities similar to aerogels. Results indicate that the primary foaming mechanism is governed by the vaporization of water that is tightly bound in secondary structures (i.e., helices, β-turns, β-sheets) that are present in dehydrated gelatin films but not present in the foams after microwave radiation (700 Watts). Full article
(This article belongs to the Special Issue Gelatin: Chemistry, Characterization, Application)
Figures

Graphical abstract

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: On-Demand Microwave-Assisted Fabrication of Gelatin Bioaerogels
Authors: Shane D. Frazier (a), Anastasia N. Aday (a), Wil V. Srubar III (a,b)
Affiliations:
1 Materials Science and Engineering Program, University of Colorado Boulder
2 Department of Civil, Environmental, and Architectural Engineering, University of Colorado Boulder, Boulder, Colorado, 80309-0428 USA
Abstract: Ultraporous gelatin bioaerogels (porosity > 94%, ρ ≈ 0.039–0.056 g/cm3) have been fabricated via microwave radiation. The resulting bioaerogels structures are unique in pore morphology (i.e., closed-cell) and exhibit 100% macroporosity (pore size 332 to 1700 μm), presence of an external skin, and densities similar to those fabricated using conventional methods (e.g., supercritical CO2, freeze drying). Results indicate that the primary foaming mechanism is governed by the vaporization of water that is tightly bound in secondary structures (i.e., helices, β-turns, β-sheets) that are present in dehydrated gelatin films but not present in the foamed bioaerogels after microwave radiation (700 Watts).
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