Endophytic bacterial communities colonizing the medicinal plant Calotropis procera: as resources of hydrolases
Calotropis procera (Aiton) W.T. Aiton is a shrub belongs to family Asclepiadaceae which known by its medicinal properties. It is a widely growing plant distributed in tropical and sub-tropical Africa, and America. This study is the first report which highlights the diversity of bacterial endophyte...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
ResearchersLinks, Ltd
2020-12-01
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| Series: | Novel Research in Microbiology Journal |
| Subjects: | |
| Online Access: | https://nrmj.journals.ekb.eg/article_130852_b66690ae925bc99591826d085315525f.pdf |
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| Summary: | Calotropis procera (Aiton) W.T. Aiton is a shrub belongs to family Asclepiadaceae which known by its
medicinal properties. It is a widely growing plant distributed in tropical and sub-tropical Africa, and America.
This study is the first report which highlights the diversity of bacterial endophytes from C. procera as sources of
numerous hydrolytic exo-enzymes. Endophytic bacteria were isolated from all plant parts such as; roots, stems,
leaves, flowers, fruits and latex. Bacillus was the prevalent genus. At the species level, the bacterial diversity was
high. Eight representative species were isolated including; Citricoccus alkalitolerans (Cps2) (NR025771),
Bacillus cereus (Cps1) (NR074540), B. pumilus (Cps3) (NR112637), B. firmus (Cpl1) (NR025842), B. niabensis
(Cpl3) (NR043334), B. subtilis (Cpl4) (NR113265), B. amyloliquefaciens (Cpl10) (NR041455) and B. subtilis
subsp. spizizenii (Cpl13) (NR112686). Results of the current study emphasized that C. procera plant hosts diverse
endophytic bacteria, which are potential producers of several economically important hydrolytic enzymes i.e.,
amylase, protease, cellulase, lipase and L-asparaginase. The aims of the current study were to identify the
endophytic bacteria associated with the different organs of the medicinal plant C. procera, and to evaluate their
potentialities to produce diverse extracellular hydrolytic enzymes. |
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| ISSN: | 2537-0286 2537-0294 |