Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine

This study was conducted to identify and characterize gelatinase bacterium of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine. The Strain G6 colony was chosen due to its high ability to hydrolyse porcine gelatine when it was grown on medium containing porcine gelatine by forming a...

Full description

Saved in:
Bibliographic Details
Main Authors: Rul Aisyah Mat Repin, Safiyyah Shahimi, Mohd Fadly Lamri, Maaruf Abdul Ghani, Sahilah Abd. Mutalib
Format: Article
Language:en
Published: Penerbit Universiti Kebangsaan Malaysia 2019
Online Access:http://journalarticle.ukm.my/14663/1/48_02_05.pdf
http://journalarticle.ukm.my/14663/
http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1834432469719318528
author Rul Aisyah Mat Repin,
Safiyyah Shahimi,
Mohd Fadly Lamri,
Maaruf Abdul Ghani,
Sahilah Abd. Mutalib,
author_facet Rul Aisyah Mat Repin,
Safiyyah Shahimi,
Mohd Fadly Lamri,
Maaruf Abdul Ghani,
Sahilah Abd. Mutalib,
author_sort Rul Aisyah Mat Repin,
building Tun Sri Lanang Library
collection Institutional Repository
content_provider Universiti Kebangsaan Malaysia
content_source UKM Journal Article Repository
continent Asia
country Malaysia
description This study was conducted to identify and characterize gelatinase bacterium of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine. The Strain G6 colony was chosen due to its high ability to hydrolyse porcine gelatine when it was grown on medium containing porcine gelatine by forming a clear zone. The bacterium was identified as Lysinibacillus spp. Strain G6 using the partial sequence of 16S rDNA analysis with 95% of similarity. Meanwhile, by using Biolog GEN III, the bacterium strain was identified as Lysinibacillus sphaericus analysis at 42% of similarity. Gelatinase from the bacterium has been partially purified using deposition of ammonium sulphate and tube dialysis. The partially purified gelatinase of Strain G6 showed significant different (p<0.05) in porcine gelatinase activity of 9.12a ± 2.6 U/ml followed by bovine (5.43b ± 0.8 U/ ml) and fish gelatine (0.14c ± 0.7 U/ml). The molecular weight of gelatinase of Strain G6 was 123.35 kDa. Application of partially purified gelatinase onto porcine, bovine and fish capsules substituted into the gelatin medium (GM), respectively resulted in 11.86a ± 0.2 U/ml, 5.39b ± 2.1 U/ml and 0.36c ± 0.2 U/ml of enzyme activity, respectively. Thus, Lysinibacillus spp. Strain G6 bacterium showed greatest gelatinase activity towards porcine gelatine which can be potentially used for porcine gelatine identification.
format Article
id my-ukm.journal.14663
institution Universiti Kebangsaan Malaysia
language en
publishDate 2019
publisher Penerbit Universiti Kebangsaan Malaysia
record_format eprints
spelling my-ukm.journal.146632020-05-21T13:39:10Z http://journalarticle.ukm.my/14663/ Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine Rul Aisyah Mat Repin, Safiyyah Shahimi, Mohd Fadly Lamri, Maaruf Abdul Ghani, Sahilah Abd. Mutalib, This study was conducted to identify and characterize gelatinase bacterium of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine. The Strain G6 colony was chosen due to its high ability to hydrolyse porcine gelatine when it was grown on medium containing porcine gelatine by forming a clear zone. The bacterium was identified as Lysinibacillus spp. Strain G6 using the partial sequence of 16S rDNA analysis with 95% of similarity. Meanwhile, by using Biolog GEN III, the bacterium strain was identified as Lysinibacillus sphaericus analysis at 42% of similarity. Gelatinase from the bacterium has been partially purified using deposition of ammonium sulphate and tube dialysis. The partially purified gelatinase of Strain G6 showed significant different (p<0.05) in porcine gelatinase activity of 9.12a ± 2.6 U/ml followed by bovine (5.43b ± 0.8 U/ ml) and fish gelatine (0.14c ± 0.7 U/ml). The molecular weight of gelatinase of Strain G6 was 123.35 kDa. Application of partially purified gelatinase onto porcine, bovine and fish capsules substituted into the gelatin medium (GM), respectively resulted in 11.86a ± 0.2 U/ml, 5.39b ± 2.1 U/ml and 0.36c ± 0.2 U/ml of enzyme activity, respectively. Thus, Lysinibacillus spp. Strain G6 bacterium showed greatest gelatinase activity towards porcine gelatine which can be potentially used for porcine gelatine identification. Penerbit Universiti Kebangsaan Malaysia 2019-05 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/14663/1/48_02_05.pdf Rul Aisyah Mat Repin, and Safiyyah Shahimi, and Mohd Fadly Lamri, and Maaruf Abdul Ghani, and Sahilah Abd. Mutalib, (2019) Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine. Malaysian Applied Biology, 48 (2). pp. 33-39. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
spellingShingle Rul Aisyah Mat Repin,
Safiyyah Shahimi,
Mohd Fadly Lamri,
Maaruf Abdul Ghani,
Sahilah Abd. Mutalib,
Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title_full Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title_fullStr Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title_full_unstemmed Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title_short Characterization of Lysinibacillus spp. (Strain G6) for hydrolysing porcine gelatine
title_sort characterization of lysinibacillus spp. (strain g6) for hydrolysing porcine gelatine
url http://journalarticle.ukm.my/14663/1/48_02_05.pdf
http://journalarticle.ukm.my/14663/
http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
url_provider http://journalarticle.ukm.my/