Partial purification and characterisation of pectinase produced by aspergillus niger LFP-1 grown on pomelo peels as a substrate

In the present study, pectinase was produced by local fungal isolate, Aspergillus niger LFP-1 grown on pomelo peels as a sole carbon source under solid-state fermentation (SSF). The purification process begins with the concentration of crude enzyme using ammonium sulfate precipitation and followed b...

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Bibliographic Details
Main Authors: Ibrahim, D. (Author), Jalil, M.T.M (Author)
Format: Article
Language:English
Published: Penerbit Universiti Sains Malaysia 2021
Series:Tropical Life Sciences Research
Subjects:
ion
Online Access:View Fulltext in Publisher
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LEADER 02474nam a2200361Ia 4500
001 10.21315-tlsr2021.32.1.1
008 220121s2021 CNT 000 0 und d
020 |a 19853718 (ISSN) 
245 1 0 |a Partial purification and characterisation of pectinase produced by aspergillus niger LFP-1 grown on pomelo peels as a substrate 
260 0 |b Penerbit Universiti Sains Malaysia  |c 2021 
490 1 |a Tropical Life Sciences Research 
650 0 4 |a Aspergillus niger 
650 0 4 |a Aspergillus niger LFP-1 
650 0 4 |a Characterisation 
650 0 4 |a chromatography 
650 0 4 |a Citrus 
650 0 4 |a Citrus maxima 
650 0 4 |a concentration (composition) 
650 0 4 |a enzyme 
650 0 4 |a experimental study 
650 0 4 |a fermentation 
650 0 4 |a fruit 
650 0 4 |a ion 
650 0 4 |a Pectinase 
650 0 4 |a purification 
650 0 4 |a Purification 
650 0 4 |a Solid state fermentation 
856 |z View Fulltext in Publisher  |u https://doi.org/10.21315/tlsr2021.32.1.1 
856 |z View in Scopus  |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-85104132263&doi=10.21315%2ftlsr2021.32.1.1&partnerID=40&md5=da06ccef4538590e94dd2c8af45603af 
520 3 |a In the present study, pectinase was produced by local fungal isolate, Aspergillus niger LFP-1 grown on pomelo peels as a sole carbon source under solid-state fermentation (SSF). The purification process begins with the concentration of crude enzyme using ammonium sulfate precipitation and followed by purification using anion-exchange column chromatography (DEAE-Sephadex) and subsequently using gel filtration column chromatography (Sephadex G-100). On the other hand, the molecular weight of the purified enzyme was determined through SDS-PAGE. The findings revealed the crude enzyme was purified up to 75.89 folds with a specific activity of 61.54 U/mg and the final yield obtained was 0.01%. The molecular mass of the purified pectinase was 48 kDa. The optimum pH and temperature were 3.5 and 50°C, respectively. This enzyme was stable at a range of pH 3.5 to 4.5 and a relatively high temperature (40°C-50°C) for 100 min. The Km and Vmax were found to be 3.89 mg/mL and 1701 U/mg, respectively. Meanwhile, pectin from citrus fruit and the metal ion (Co2+) were the best substrate and inducer to enhance pectinase yield, respectively. © Penerbit Universiti Sains Malaysia, 2021. 
700 1 0 |a Ibrahim, D.  |e author 
700 1 0 |a Jalil, M.T.M.  |e author 
773 |t Tropical Life Sciences Research