Microbial alkaline protease from animal waste: Immobilization and characterization

Alkaline protease (AP) produced from protein-rich animal waste as chicken feather (CF) and fish fin (FF) by mixed culture was immobilized and characterized. The immobilized enzyme activity obtained in 0.25g beads was 0.398 and 0.411 (U/mL) for CF and FF respectively. Besides; the initial activity wa...

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Main Authors:	Raid D., Thanoon, Makky, Essam A., M. M., Yusoff
Format:	Conference or Workshop Item
Language:	English English
Published:	2018
Subjects:	QD Chemistry
Online Access:	http://umpir.ump.edu.my/id/eprint/21975/ http://umpir.ump.edu.my/id/eprint/21975/1/25.%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf http://umpir.ump.edu.my/id/eprint/21975/2/25.1%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf

id	ump-21975
recordtype	eprints
spelling	ump-219752018-09-21T02:08:27Z http://umpir.ump.edu.my/id/eprint/21975/ Microbial alkaline protease from animal waste: Immobilization and characterization Raid D., Thanoon Makky, Essam A. M. M., Yusoff QD Chemistry Alkaline protease (AP) produced from protein-rich animal waste as chicken feather (CF) and fish fin (FF) by mixed culture was immobilized and characterized. The immobilized enzyme activity obtained in 0.25g beads was 0.398 and 0.411 (U/mL) for CF and FF respectively. Besides; the initial activity was 0.424±0.011 and 0.417±0.017 (U/mL) from the extracted protein, accordingly. While enzyme activity entrapped in 0.25g beads was 0.081 and 0.151 (U/ml), respectively. The beads protein content at 4 cycles up to 0.171±0.001 and 0.176±0.006 (mg/ml), respectively and gradually decreased through the second run by approximately 10% and ended up with 40% activity loss 0.124±0.002 and 0.112±0.003 (mg/ml) accordingly. The enzyme showed zero % activity loss for the first cycle and gradually decreased along the fourth cycle. The storage stability of the enzyme was recorded at 1st day 0.424 ± 0.011 and 0.417 ± 0.017 (U/mL) as the initial activity of AP, respectively, while the activity for the 5th day 0.167 ± 0.004 and 0.167 ± 0.003 (U/mL) were used as the final activity of the immobilized and free enzymes, respectively. 2018-03 Conference or Workshop Item NonPeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/21975/1/25.%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf pdf en http://umpir.ump.edu.my/id/eprint/21975/2/25.1%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf Raid D., Thanoon and Makky, Essam A. and M. M., Yusoff (2018) Microbial alkaline protease from animal waste: Immobilization and characterization. In: The 2nd International Conference On Sustainable Energy Engineering (ICSEE 2018), 15 - 17 Jun 2018 , Sydney, Australia. pp. 1-5.. (Unpublished)
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English English
topic	QD Chemistry
spellingShingle	QD Chemistry Raid D., Thanoon Makky, Essam A. M. M., Yusoff Microbial alkaline protease from animal waste: Immobilization and characterization
description	Alkaline protease (AP) produced from protein-rich animal waste as chicken feather (CF) and fish fin (FF) by mixed culture was immobilized and characterized. The immobilized enzyme activity obtained in 0.25g beads was 0.398 and 0.411 (U/mL) for CF and FF respectively. Besides; the initial activity was 0.424±0.011 and 0.417±0.017 (U/mL) from the extracted protein, accordingly. While enzyme activity entrapped in 0.25g beads was 0.081 and 0.151 (U/ml), respectively. The beads protein content at 4 cycles up to 0.171±0.001 and 0.176±0.006 (mg/ml), respectively and gradually decreased through the second run by approximately 10% and ended up with 40% activity loss 0.124±0.002 and 0.112±0.003 (mg/ml) accordingly. The enzyme showed zero % activity loss for the first cycle and gradually decreased along the fourth cycle. The storage stability of the enzyme was recorded at 1st day 0.424 ± 0.011 and 0.417 ± 0.017 (U/mL) as the initial activity of AP, respectively, while the activity for the 5th day 0.167 ± 0.004 and 0.167 ± 0.003 (U/mL) were used as the final activity of the immobilized and free enzymes, respectively.
format	Conference or Workshop Item
author	Raid D., Thanoon Makky, Essam A. M. M., Yusoff
author_facet	Raid D., Thanoon Makky, Essam A. M. M., Yusoff
author_sort	Raid D., Thanoon
title	Microbial alkaline protease from animal waste: Immobilization and characterization
title_short	Microbial alkaline protease from animal waste: Immobilization and characterization
title_full	Microbial alkaline protease from animal waste: Immobilization and characterization
title_fullStr	Microbial alkaline protease from animal waste: Immobilization and characterization
title_full_unstemmed	Microbial alkaline protease from animal waste: Immobilization and characterization
title_sort	microbial alkaline protease from animal waste: immobilization and characterization
publishDate	2018
url	http://umpir.ump.edu.my/id/eprint/21975/ http://umpir.ump.edu.my/id/eprint/21975/1/25.%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf http://umpir.ump.edu.my/id/eprint/21975/2/25.1%20Microbial%20alkaline%20protease%20from%20animal%20waste%20Immobilization.pdf
first_indexed	2023-09-18T22:32:29Z
last_indexed	2023-09-18T22:32:29Z
_version_	1777416378243874816

Microbial alkaline protease from animal waste: Immobilization and characterization

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