Evidence map›Paper›PMID 32455881›Full record

ReviewInternational journal of molecular sciences2020

Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics.

C Valeria L Giosafatto, Antonio Fusco, Asmaa Al-Asmar, Loredana Mariniello

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 32 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

C Valeria L GiosafattoDepartment of Chemical Sciences, University of Naples "Federico II", 80126 Naples, Italy.ORCID 0000-0001-8762-2205
Antonio FuscoUnità Operativa Struttura Complessa Medicina di Laboratorio, Presidio Ospedaliero Santa Maria di Loreto Nuovo, ASL Na1 Centro, 80145 Naples, Italy.
Asmaa Al-AsmarDepartment of Chemical Sciences, University of Naples "Federico II", 80126 Naples, Italy.ORCID 0000-0003-0751-6301
Loredana MarinielloDepartment of Chemical Sciences, University of Naples "Federico II", 80126 Naples, Italy.ORCID 0000-0002-6800-5890
University of Naples Federico II · ITAn-Najah National University · PSPresidio Ospedaliero · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several proteins from animal and plant origin act as microbial transglutaminase substrate, a crosslinking enzyme capable of introducing isopeptide bonds into proteins between the aminoacids glutamines and lysines. This feature has been widely exploited to modify the biological properties of many proteins, such as emulsifying, gelling, viscosity, and foaming. Besides, microbial transglutaminase has been used to prepare bioplastics that, because made of renewable molecules, are able to replace the high polluting plastics of petrochemical origin. In fact, most of the time, it has been shown that the microbial enzyme strengthens the matrix of protein-based bioplastics, thus, influencing the technological characteristics of the derived materials. In this review, an overview of the ability of many proteins to behave as good substrates of the enzyme and their ability to give rise to bioplastics with improved properties is presented. Different applications of this enzyme confirm its important role as an additive to recover high value-added protein containing by-products with a double aim (i) to produce environmentally friendly materials and (ii) to find alternative uses of wastes as renewable, cheap, and non-polluting sources. Both principles are in line with the bio-economy paradigm.

Indexed as

AnimalsBiodegradation, EnvironmentalBiotechnologyCollagenColloidsEgg ProteinsEnvironmental PollutionGlutamineLysineMilk ProteinsPectinsPlant ProteinsPlasticsTransglutaminasesCollagenColloidsEgg ProteinsGlutamineLysineMilk ProteinsPectinsPlant ProteinsPlasticsTransglutaminasesbioplasticsedible filmsenzymatic strengtheningplastic pollutiontechnological properties

Identifiers

PMID32455881
PMCPMC7279461
OpenAlexW3026698916

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.