Evidence map›Paper›PMID 32705554›Full record

ArticleEnvironmental science and pollution research international2020

α-Amylase production by Tepidimonas fonticaldi strain HB23: statistical optimization and compatibility study for use in detergent formulations.

Fawzi Allala, Khelifa Bouacem, Nawel Boucherba, Sondes Mechri, Mouna Kriaa, Warda Arkoub-Djoudi, Zahra Azzouz, Said Benallaoua, Hocine Hacene, Bassem Jaouadi and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Environmental science and pollution research international, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Detergent-stable amylase production byBiotechnology reports (Amsterdam, Netherlands) · 2023
    Article
  3. Optimization of β-1,4-Endoxylanase Production by anMolecules (Basel, Switzerland) · 2021
    Article
  4. Article
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

11 authors at 4 institutions in 2 countries.

Fawzi AllalaLaboratory of Cellular and Molecular Biology, Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111, Algiers, Algeria. allala.fawzi@gmail.com.
Khelifa BouacemLaboratory of Cellular and Molecular Biology, Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111, Algiers, Algeria.
Nawel BoucherbaLaboratory of Applied Microbiology, Faculty of Nature and Life Sciences, University of Bejaïa, Targa Ouzemmour, 06000, Bejaïa, Algeria.
Sondes MechriLaboratory of Microbial Biotechnology, Enzymatic, and Biomolecules, Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, 3018, Sfax, Tunisia.
Mouna KriaaLaboratory of Microbial Biotechnology, Enzymatic, and Biomolecules, Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, 3018, Sfax, Tunisia.
Warda Arkoub-DjoudiLaboratory of Applied Microbiology, Faculty of Nature and Life Sciences, University of Bejaïa, Targa Ouzemmour, 06000, Bejaïa, Algeria.
Zahra AzzouzLaboratory of Applied Microbiology, Faculty of Nature and Life Sciences, University of Bejaïa, Targa Ouzemmour, 06000, Bejaïa, Algeria.
Said BenallaouaLaboratory of Applied Microbiology, Faculty of Nature and Life Sciences, University of Bejaïa, Targa Ouzemmour, 06000, Bejaïa, Algeria.
Hocine HaceneLaboratory of Cellular and Molecular Biology, Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111, Algiers, Algeria.
Bassem JaouadiLaboratory of Microbial Biotechnology, Enzymatic, and Biomolecules, Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, 3018, Sfax, Tunisia.
Amel Bouanane-DarenfedLaboratory of Cellular and Molecular Biology, Microbiology Team, Faculty of Biological Sciences, University of Sciences and Technology Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111, Algiers, Algeria. amelbouanane@gmail.com.
University of Béjaïa · DZUniversity of Sciences and Technology Houari Boumediene · DZUniversity of Sfax · TNCentre of Biotechnology of Sfax · TN

Funding

Direction Générale de la Recherche Scientifique et du Développement Technologique PRFU_code D01N01UN160420180023Multilateral project PHC-Maghreb 2020 program FranMaghZYM, N°43791TM 2019-2023 code 01MAG20
6 · The paper itself

Abstract

In a previous study, a thermostable α-amylase-producing bacterium (designated HB23) was isolated from an Algerian hydrothermal spring. In the present study, the native strain was subjected to a statistical optimization aimed at enhancing the α-amylase production. To achieve this, thirteen factors have been studied, among which are cultural and nutritional parameters. Wheat bran, a by-product of the grain milling industry, was the factor that positively influenced α-amylase production. A modified L27 Taguchi design was used to screen these factors. Furthermore, a Box-Behnken matrix, supplemented by the use of response surface methodology (RSM), allowed for the identification of optimum levels of the following factors: a 1% inoculum size, 15 g/L soluble starch, 5 g/L wheat bran, and 1 g/L tryptone. Optimized conditions resulted in an amylolytic activity of 320 U/mL, which is a tenfold increase when compared with unoptimized production level. Phenotypical and molecular identification of strain HB23 revealed its close relationship to various Tepidimonas strains, specifically to Tepidimonas fonticaldi. The crude enzyme preparation turned out to be compatible with various laundry detergents and led to a substantial improvement in their washing performance. A comparison of the performance of the crude enzyme preparation with that of the commercial α-amylase (Termamyl

Indexed as

alpha-AmylasesDetergentsBurkholderialesDietary FiberStarchalpha-AmylasesDetergentsDietary FiberStarchBox-Behnken designCrude amylaseHot springResponse surface methodologyTaguchi designTermamyl® 300 LWheat bran

Identifiers

PMID32705554
OpenAlexW3044407950

What OpenQuestion holds

Textmetadata
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.