Gene expression of microbial gelatinase activity for porcine gelatine identification.

Autor: Shahimi S; Universiti Teknologi MARA, Cawangan Negeri Sembilan, Kampus Kuala Pilah, 72000 Kuala Pilah, Malaysia; Department of Food Science, Faculty of Science and Technology, 43600 Universiti Kebangsaan Malaysia, Bangi, Malaysia., Lamri MF; Politeknik METrO Kuantan, No A-5 Jalan Tun Ismail 2, Sri Dagangan 11, 25000 Kuantan Pahang, Malaysia., Abd Mutalib S; Department of Food Science, Faculty of Science and Technology, 43600 Universiti Kebangsaan Malaysia, Bangi, Malaysia; Innovation Centre for Confectionery Technology (MANIS), Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: sahilah@ukm.edu.my., Mohd Khalid R; Department of Chemistry, Faculty of Science and Technology, 43600 Universiti Kebangsaan Malaysia, Bangi, Malaysia., Md Tab M; Jabatan Kimia Malaysia, Jalan Sultan, 46661 Petaling Jaya, Selangor, Malaysia., Khairuddin F; Malaysia Genome Institute (MGI), Jalan Bangi, 43000 Kajang, Selangor, Malaysia.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2021 Sep 01; Vol. 355, pp. 129586. Date of Electronic Publication: 2021 Mar 13.
DOI: 10.1016/j.foodchem.2021.129586
Abstrakt: In order to invent a porcine gelatine detection device using microbial resources, bacterial enzymes with a preference towards porcine gelatine and their candidate genes were evaluated. Five (n = 5) bacterial strains isolated from hot spring water and wet clay, Malaysia were screened for their gelatinase activity. The gelatinase enzyme was extracted and purified using ammonium sulphate precipitation prior to performing gelatinase assay on porcine, bovine and fish gelatine medium substrates. The G2 strain or Enterobacter aerogenes (Strain EA1) was selected for whole genome sequenced after showing a consistent trend of preference towards porcine gelatine. The gelatinase candidate gene gelEA1_9 was cloned and expressed. Based on one-way analysis of variance (ANOVA) with POST-HOC Duncan test (α = 0.05), the final product of gelEA1_9 was identified as a novel gelatinase. This gelatinase presented no significant difference in activity towards porcine gelatine. Hence, the present study demonstrated an enzyme-substrate interaction for porcine gelatine identification.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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