CiteULike CiteULike
Delicious Delicious
Connotea Connotea

Citation for Study 30171

Reviewer/Referee Access Agreement

You have reached this page using a special URL that is intended to be used by journal editors and reviewers or referees of a paper that is under consideration for publication. This URL gives you access to the submitted data and metadata associated with analyses and results presented in the paper under review. Please carefully examine the data paying special attention to the following:
  • The citation data (authors, year, citation, abstract) should be complete, except for information that is not yet known (e.g. volume or page numbers).
  • Verify that nexus files are error-free and executable by software programs (e.g. PAUP, Mesquite, MacClade, etc). Please make sure that the taxon labels for trees are identical, or a subset of, the taxon labels in data matrices connected by way of an analysis. If taxon labels in trees do not match with taxon labels in associated data matrices, the data will not be useful to the scientific community.
  • Verify that data are not missing and that opportunities to supply valuable metadata are not overlooked. For example, TreeBASE can store Genbank accession numbers, museum voucher IDs, latitude and longitudes for specimen localities, character names and character state names for morphological data, etc. Including these metadata are sometimes overlooked by submitting authors, yet sharing this metadata is extremely valuable to the scientific community. Please use your power as a reviewer to encourage the sharing of richly-annotated metadata.
  • Verify that analyses are not missing and that, where possible, analysis entries include software commands (e.g. the contents of a PAUP block or MrBayes block) so that analyses can be replicated easily (e.g. commands that describe substitution models, data partitions, and heuristic search parameters).
  • Verify that taxon labels are mapped against TreeBASE's taxonomic dictionary. Data in TreeBASE can only be found using a taxon name search if the taxon labels are properly mapped.
By clicking the 'OK' button below, you agree to keep these data confidential; you agree not to retain these data after completing your report to the journal editor; you agree not to use these data or knowledge of these data for the purposes of your research until and unless the paper under review has been published and the data have been made available to the general public; you agree to keep the URL confidential.
About Citation title: "Production of cold‑active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme".
About Study name: "Production of cold‑active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme".
About This study is part of submission 30171 (Status: In Progress).

Citation

Moharram A.M., Zohri A.A., Hesham A., Abdel-raheam H.E., Maher M.A., & Al-bedak O.A. 2022. Production of cold‑active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme. , 12: 17.

Authors

  • Moharram A.M.
  • Zohri A.A.
  • Hesham A.
  • Abdel-raheam H.E.
  • Maher M.A.
  • Al-bedak O.A.

Abstract

Cladosporium parasphaerospermum, Cladosporium chlamydosporigenum, and Cladosporium compactisporum have all been discovered and characterized as new Cladosporium species. The three new species seemed to generate cold‑active pectinases with high activity at pH 6.0 and 10 ?C, pH 6.0 and 15 ?C, and pH 5.0 and 15 ?C, respectively, with the most active being C. parasphaerospermum pectinase. In submerged fermentation (SmF), C. parasphaerospermum produced the most cold‑active pectinase with the highest activity and specific activity (28.84 U/mL and 3797 U/mg) after 8 days. C. parasphaerospermum cold‑active pectinase was isolated using DEAE‑Cellulose anion exchange resin and a Sephadex G 100 gel filtration column. The enzyme was purified 214.4‑fold and 406.4‑fold greater than the fermentation medium using DEAE‑cellulose and Sephadex G 100, respectively. At pH 7.0 and 10 ?C, pure pectinase had the highest activity (6684 U/mg), with Km and Vmax determined to be 26.625 mg/mL and 312.5 U/min, respectively. At 5 mM/mL, EDTA, MgCl2, and SDS inhibited the activity of pure pectinase by 99.21, 96.03, and 94.45%, respectively. The addition of 10 U/mL pure pectinase enhanced the yield of apple, orange, apricot, and peach juice by 17, 20, 13, and 24%, respectively, and improved the clarity and colour of orange juice by 194 and 339%, respectively. We can now add cold‑active pectinase production to the long list of Cladosporium species that have been identified. We also report three new species that can be used in biotechnological solutions as active microbial pectinase producers. Although further research is needed, these distinct species might be used to decompose difficult and resistant pertinacious wastes as well as clear fruit juices.

External links

About this resource

  • Canonical resource URI: http://purl.org/phylo/treebase/phylows/study/TB2:S30171
  • Other versions: Download Reconstructed NEXUS File Nexus Download NeXML File NeXML
  • Show BibTeX reference
  • Show RIS reference