Asia Life Sciences

(ISSN: 01173375)

Asia Life Sciences (ISSN: 01173375) - is an international peer reviewed scientific journal which is devoted to the publication of original research in the Life Sciences and related disciplines. Articles originating from anywhere in the world are most welcome.

Volume - 12 , Issue 11
20 Dec 2022
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Upcoming Publication
Volume - 12 , Issue 09
30 Sep 2022

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Aim and Scope

ASIA LIFE SCIENCES (ISSN: 01173375) - is an international peer reviewed scientific journal which is devoted to the publication of original research in the Life Sciences and related disciplines. Articles originating from anywhere in the world are most welcome. AMA, Agricultural Mechanization in Asia, Africa and Latin America Teikyo Medical Journal Journal of the Mine Ventilation Society of South Africa Dokkyo Journal of Medical Sciences Zhonghua er bi yan hou tou jing wai ke za zhi = Chinese journal of otorhinolaryngology head and neck surgery Interventional Pulmonology

Scope : Agricultural Science, Biochemistry, Biology, Bioinformatics, Botany, Cytology, Cell biology, Chemistry, Ecology, Endocrinology, Entomology, Environmental Sciences, Food science and Technology, Genetics, Genomics & Proteomics, mmunobiology, Molecular biology, Marine Science, Microbiology, Neurobiology, Pathology, Physics, Physiology, Psychology, Veterinary Science, Zoology .

Latest Journals

Identification of transcription factors and DNA-binding domains with conservation analysis of the 5'-upstream promoter sequence of Chitinase-3-like protein-1 (CHI3L1) gene encoding YKL-40 protein: A type-2-diabetes specific inflammatory glycoprotein marker
Journal ID : ALS-27-09-2022-5645; Total View : 25; Author : Raj Rani, Varsha Singh,
Abstract : YKL-40, encoded by Chitinase-3-like protein 1 (CHI3L1) gene, is predominantly an inflammation-based secretory glycoprotein in type-2-diabetes. The transcriptional mechanism, especially the upstream promoter region of the human CHI3L1 gene, remains unknown. The aim was to performin silico upstream promoter identification and analysis to determine types of transcription factors and their binding domains crucial in transcribing the human CHI3L1 gene along with multiple sequence alignments and detailed phylogenetic analysis of eight mammalian species of the CHI3L1 gene. The key finding revealed that YKL-40 is regulated by inflammation-based transcription factors, which are positive regulators mostly signal-dependent belonging to basic-, zinc-coordinating- and helix-turn-helix -DNA-binding domains. Phylogenetic analysis reveals that the promoter region of the primate species evolved together. The 5’-upstream promoter regions lying within the -3000 bp of the transcription start site are highly dynamic regions to bind transcription factors and consist of their respective transcription factor binding domains.
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PRODUCTION AND OPTIMIZATION OF EXTRACELLULAR XYLANASE ACTIVITY FROM A THERMOPHILIC ACTINOMYCETE ISOLATED FROM POULTRY COMPOST (EAST- ALGERIA)
Journal ID : ALS-19-09-2022-5644; Total View : 193; Author : Habbeche Amina, Haberra Soumaya, Kerouaz Bilal, Saoudi Boudjema, Ladjama Ali,
Abstract : From 32 isolates of actinomycetes isolated from poultry compost in Annaba (East Area Algeria), three autochthones strains Cpt20, Cpt8, Cpt29 screened for their ability of producing thermostable xylanase activities based on the diameter of the clear zone formation in birchwood xylan agar plates. One of them, as Actinomadura keratinilytica Cpt20 produced high amount of extracellular xylanases, this strain was selected and optimized for xylanase enzyme produced in liquid state fermentation. Consequently, for commercial applications, it is advisable to develop processes production starting from inexpensive substrates. The presence of wheat bran as a carbon source in the medium induced the highest production of xylanase (30.64IU/ml). This result is particulary valuable because the other substrates are more expensive. Among all the organic and inorganic sources of nitrogen tested in the study, peptone was found to be the best in stimulating xylanase produced by Actinomadura keratinilytica Cpt20. Optimum pH and temperature for xylanase activity were found to be 8.5 and 45°C after 72h of incubation. After optimization of various production parameters, an increase of nearly 2-fold in xylanase production was achieved. The enzyme has an optimal temperature at 70°C and the half-life of the xylanase at 75°C was 30min.
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