Determination Of Proteolytic Activity Of Bacillus Species Isolated From Ugba.

ORJI VICTORIA AMARACHUKWU | 67 pages (11866 words) | Projects

ABSTRACT

Eighty samples of traditionally fermented oil bean seeds (ugba) were analyzed for the presence of Bacillus species with proteolytic activity. Eight (80) isolates were recovered; fifty-one were identified as B. subtilis, eighteen as B. licheniformis and eleven as B. subilus. The protcolytic activities of these species of Bacillus were investigated using two protein-based substrates: skim milk agar and nutrient agar supplemented with % gelatin. When tested on these media. B. licheniformiis and B. subtilis were found to exhibit the highest proleolytic activity (ranging from 26 to 27 mm) (P<0.05) on nutrient agar supplemented with 1% gelatin: whereas, on skim milk agar. B. subtilis has a higher proteolytic activity (between 27 to 2 mm) (P><0.05) than B. licheniforinis; while, B. piiinilus gave the lowest proteol tic acti vilv on both media (between 11 to 13 mm). 'l'he two potential protease producers that showed high proteolylic activity were subjected to protease production at high temperature incubation at a constant pt-t of . However. Bs u/,tilis gave its maximal proteol tic activity at 50°C while B. liciwni/ornus gave its maximal protease activity at 40°C respectively and there was a reduction in the protease activity at on nutrient agar supplemented with 1% gelatin: whereas, on skim milk agar. B. subtilis has a higher proteolytic activity (between 27 to 2 mm) (P<0.05) than B. licheniforinis; while, B. piiinilus gave the lowest proteol tic acti vilv on both media (between 11 to 13 mm). 'l'he two potential protease producers that showed high proteolylic activity were subjected to protease production at high temperature incubation at a constant pt-t of . However. Bs u/,tilis gave its maximal proteol tic activity at 50°C while B. liciwni/ornus gave its maximal protease activity at 40°C respectively and there was a reduction in the protease activity at ) than B. licheniformis; while, B. piiinilus gave the lowest proteolytic activilv on both media (between 11 to 13 mm). 'the two potential protease producers that showed high proteolylic activity were subjected to protease production at high temperature incubation at a constant pH of . However. B. subtiis  gave its maximal proteolytic activity at 50°C while B. licheniformis gave its maximal protease activity at 40°C respectively and there was a reduction in the protease activity at 60°C' for both species. The antimicrobial susceptibility test of these Bucillus species were also determined, the three species of Bacillus were susceptible to gentamicin. amoxil. chioramphenicol and ampiclox. whereas. they are resistant to rifampicin. Two species of Bacillus were found to possess good proteolylic activities at high temperatures and these will be of good application in industry where high temperature is needed

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APA

ORJI, A (2021). Determination Of Proteolytic Activity Of Bacillus Species Isolated From Ugba.. Mouau.afribary.org: Retrieved Nov 16, 2024, from https://repository.mouau.edu.ng/work/view/determination-of-proteolytic-activity-of-bacillus-species-isolated-from-ugba-7-2

MLA 8th

AMARACHUKWU, ORJI. "Determination Of Proteolytic Activity Of Bacillus Species Isolated From Ugba." Mouau.afribary.org. Mouau.afribary.org, 04 Aug. 2021, https://repository.mouau.edu.ng/work/view/determination-of-proteolytic-activity-of-bacillus-species-isolated-from-ugba-7-2. Accessed 16 Nov. 2024.

MLA7

AMARACHUKWU, ORJI. "Determination Of Proteolytic Activity Of Bacillus Species Isolated From Ugba.". Mouau.afribary.org, Mouau.afribary.org, 04 Aug. 2021. Web. 16 Nov. 2024. < https://repository.mouau.edu.ng/work/view/determination-of-proteolytic-activity-of-bacillus-species-isolated-from-ugba-7-2 >.

Chicago

AMARACHUKWU, ORJI. "Determination Of Proteolytic Activity Of Bacillus Species Isolated From Ugba." Mouau.afribary.org (2021). Accessed 16 Nov. 2024. https://repository.mouau.edu.ng/work/view/determination-of-proteolytic-activity-of-bacillus-species-isolated-from-ugba-7-2

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