Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application
Lactic acid bacteria (LAB) are known to produce extracellular enzymes that could be exploited for use in the dairy industry. Ten of 135 LAB isolated from different food sources produced extracellular enzyme of which six LAB isolates from Malaysian fermented foods (belacan, pekasam, budu, fermente...
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| id |
my-usim-ddms-13028 |
|---|---|
| record_format |
uketd_dc |
| institution |
Universiti Sains Islam Malaysia |
| collection |
USIM Institutional Repository |
| language |
English |
| topic |
Lactic acid bacteria (LAB) Food -- research -- technology |
| spellingShingle |
Lactic acid bacteria (LAB) Food -- research -- technology Mohamed Muftah Ahmad Imdakim Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| description |
Lactic acid bacteria (LAB) are known to produce extracellular enzymes that could be
exploited for use in the dairy industry. Ten of 135 LAB isolated from different food
sources produced extracellular enzyme of which six LAB isolates from Malaysian
fermented foods (belacan, pekasam, budu, fermented buffalo milk and fermented
ginger) produced milk clotting activity (MCA). The MCA of the isolates ranged
between 30 and 50 SU/ml. The six isolates were identified by (API 50CHL) and
confirmed by the sequence analysis of 16S rDNA gene as Pediococcus acidilactici
SH, Lactobacillus paracasei CF1 Lactobacillus plantaruni ASC 1, L. plantaraan H6M,
Enterococcus faecium FFA, and Enterococcus faecium FFB. High MCA of 50.0 (SU/
ml) and 43.0 (SU/ ml) were shown by P. acidilactici SH and L. paracasei CF1,
respectively and were chosen for further analysis. Nitrogen sources, pH and
temperature significantly (p<0.05) influenced the MCA of enzymes produced by the
two LAB. Among the nitrogen sources namely, casein, tryptophan, trypticase peptone
and tryptone soya added to the enzyme production media, casein was found to
increase significantly (p<0.05) the MCA to (75SU/ ml) for P. acidilactici SH and 57.0
(SU/ ml) for L. paracasei CFI, at casein concentration 0.5 % and 1%, respectively.
The optimum pH and temperatures for maximum MCA were pH 6 and 50 °C for P.
acidilactici SH and pH 7 and 40 °C for L. paracasei CFI. SDS-PAGE of the purified
enzyme by ammonium sulfate and Sephadex G-50 fine produced bands with a
molecular weight of approximately 30 KDa and 27 KDa for P. acidilactici SH and L.
paracasei CF1, respectively. Urea SDS-PAGE analysis showed that MCE produce by
L. paracasei CF1 hydrolysed x-casein and incomplete degradation of a and 0-casein,
while MCE produce by P. acidilactici SH was active on x-casein but not on a and ßcasein.
Addition of freeze dried enzyme (1% w/v) to goat milk and skim milk (12.5%
w/v) successfully produced a dadih with the acceptable texture properties. This study
indicates the possibility of exploiting LAB from food sources for the production of
milk-clotting enzymes for dairy production |
| format |
Thesis |
| author |
Mohamed Muftah Ahmad Imdakim |
| author_facet |
Mohamed Muftah Ahmad Imdakim |
| author_sort |
Mohamed Muftah Ahmad Imdakim |
| title |
Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| title_short |
Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| title_full |
Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| title_fullStr |
Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| title_full_unstemmed |
Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application |
| title_sort |
characterization and purification of milk clotting enzyme from lactic acid bacteria and it’s application |
| granting_institution |
Universiti Sains Islam Malaysia |
| url |
https://oarep.usim.edu.my/bitstreams/60e5ee52-0aaf-4233-bf6d-9dca523bc791/download https://oarep.usim.edu.my/bitstreams/e5b3f690-ece1-45fd-9e9d-ee7a4160e0ac/download https://oarep.usim.edu.my/bitstreams/f495d2c5-2358-479d-9811-c653a4259efb/download https://oarep.usim.edu.my/bitstreams/6e937e5a-8c28-4ca9-ad86-0a6b24e1f23d/download https://oarep.usim.edu.my/bitstreams/c27c9821-7f9d-4052-862a-ba8fe6f1d9b2/download https://oarep.usim.edu.my/bitstreams/e787b4fd-caf8-40e9-8df2-ff62bcd0cf18/download https://oarep.usim.edu.my/bitstreams/22bbe44b-a79d-459a-bc51-f5e0cbe2edcd/download https://oarep.usim.edu.my/bitstreams/22a5584b-4763-4693-a1cd-c6df343ce85b/download https://oarep.usim.edu.my/bitstreams/2c5b949a-604b-45b0-93ee-379f2d9be935/download https://oarep.usim.edu.my/bitstreams/4676c22f-63f9-4a1a-8f90-8ce70726efbb/download |
| _version_ |
1812444775295483904 |
| spelling |
my-usim-ddms-130282024-05-29T19:08:05Z Characterization And Purification Of Milk Clotting Enzyme From Lactic Acid Bacteria And It’s Application Mohamed Muftah Ahmad Imdakim Lactic acid bacteria (LAB) are known to produce extracellular enzymes that could be exploited for use in the dairy industry. Ten of 135 LAB isolated from different food sources produced extracellular enzyme of which six LAB isolates from Malaysian fermented foods (belacan, pekasam, budu, fermented buffalo milk and fermented ginger) produced milk clotting activity (MCA). The MCA of the isolates ranged between 30 and 50 SU/ml. The six isolates were identified by (API 50CHL) and confirmed by the sequence analysis of 16S rDNA gene as Pediococcus acidilactici SH, Lactobacillus paracasei CF1 Lactobacillus plantaruni ASC 1, L. plantaraan H6M, Enterococcus faecium FFA, and Enterococcus faecium FFB. High MCA of 50.0 (SU/ ml) and 43.0 (SU/ ml) were shown by P. acidilactici SH and L. paracasei CF1, respectively and were chosen for further analysis. Nitrogen sources, pH and temperature significantly (p<0.05) influenced the MCA of enzymes produced by the two LAB. Among the nitrogen sources namely, casein, tryptophan, trypticase peptone and tryptone soya added to the enzyme production media, casein was found to increase significantly (p<0.05) the MCA to (75SU/ ml) for P. acidilactici SH and 57.0 (SU/ ml) for L. paracasei CFI, at casein concentration 0.5 % and 1%, respectively. The optimum pH and temperatures for maximum MCA were pH 6 and 50 °C for P. acidilactici SH and pH 7 and 40 °C for L. paracasei CFI. SDS-PAGE of the purified enzyme by ammonium sulfate and Sephadex G-50 fine produced bands with a molecular weight of approximately 30 KDa and 27 KDa for P. acidilactici SH and L. paracasei CF1, respectively. Urea SDS-PAGE analysis showed that MCE produce by L. paracasei CF1 hydrolysed x-casein and incomplete degradation of a and 0-casein, while MCE produce by P. acidilactici SH was active on x-casein but not on a and ßcasein. Addition of freeze dried enzyme (1% w/v) to goat milk and skim milk (12.5% w/v) successfully produced a dadih with the acceptable texture properties. This study indicates the possibility of exploiting LAB from food sources for the production of milk-clotting enzymes for dairy production Universiti Sains Islam Malaysia 2016-01 Thesis en https://oarep.usim.edu.my/handle/123456789/13028 https://oarep.usim.edu.my/bitstreams/772266da-65ca-4b90-ba1f-3254c88dc32e/download 8a4605be74aa9ea9d79846c1fba20a33 https://oarep.usim.edu.my/bitstreams/60e5ee52-0aaf-4233-bf6d-9dca523bc791/download d93072d516a1fab412d45e474d1959ee https://oarep.usim.edu.my/bitstreams/e5b3f690-ece1-45fd-9e9d-ee7a4160e0ac/download e0b8d0705de793d011cef549b36ec0bf https://oarep.usim.edu.my/bitstreams/f495d2c5-2358-479d-9811-c653a4259efb/download f2e89ffe908b222985ac4a0ac335b14d https://oarep.usim.edu.my/bitstreams/6e937e5a-8c28-4ca9-ad86-0a6b24e1f23d/download 444ff8c5e50189e0ea6555a6805dae10 https://oarep.usim.edu.my/bitstreams/c27c9821-7f9d-4052-862a-ba8fe6f1d9b2/download dee472e8466dccced2922f325fc2461b https://oarep.usim.edu.my/bitstreams/e787b4fd-caf8-40e9-8df2-ff62bcd0cf18/download 0473406aeae07fdfdd63f8ce2a42efbe https://oarep.usim.edu.my/bitstreams/22bbe44b-a79d-459a-bc51-f5e0cbe2edcd/download 94639bf3c74ade96692317244aa26233 https://oarep.usim.edu.my/bitstreams/22a5584b-4763-4693-a1cd-c6df343ce85b/download 2fbd5b412ebf43221cdaeef53075f439 https://oarep.usim.edu.my/bitstreams/2c5b949a-604b-45b0-93ee-379f2d9be935/download e898b12f59592070b736ff2847411d8e https://oarep.usim.edu.my/bitstreams/4676c22f-63f9-4a1a-8f90-8ce70726efbb/download 0deb506415c71bfda254dbb5b9453eab https://oarep.usim.edu.my/bitstreams/d6c8cf04-60ea-42e2-bbbc-8be2a48c8d28/download a0c74c6db3667e59cc95ef74741ab35d https://oarep.usim.edu.my/bitstreams/3e967560-a764-4bdb-9b1e-0665778d2573/download 9027fed24669b9d7438f0300f57b926b https://oarep.usim.edu.my/bitstreams/a3dc5a5d-345a-42e9-8273-6977fd5efc0e/download 26639097ddfae52cfba5baced89b3655 https://oarep.usim.edu.my/bitstreams/19224865-023f-4e18-8497-7cb397712ff1/download e60abfc9c48fd5b57ce579064d75a038 https://oarep.usim.edu.my/bitstreams/6dc4dec6-b102-4cdb-a6dc-05b329ce1cde/download d329d53c4c7cb2770ef2c7d986a3f8fe https://oarep.usim.edu.my/bitstreams/e487e468-cc8a-4bbe-bca0-92daa87e64c1/download 32eac3ee1233d3c96e933b4c3ca5eb48 https://oarep.usim.edu.my/bitstreams/b30f5ba1-2520-45b1-bdcc-a6f18bb9e79f/download 14bb1cf9364f65d0d34405a5bb385c2b https://oarep.usim.edu.my/bitstreams/4d5d38c2-d8cf-4f0e-ba0d-a1a07e2431ee/download 4f567defd04db2cc40ad19943ca7c80f https://oarep.usim.edu.my/bitstreams/c8d43f96-fa2b-4259-8d28-814467be463e/download 7c7ef5d641c7acd9dd260102a778d2a4 https://oarep.usim.edu.my/bitstreams/432ffaa4-d1e2-486a-8f17-c126a6a3f815/download fa750061a516e6e3e25517ac4e138178 Lactic acid bacteria (LAB) Food -- research -- technology |