Extracellular amylase activity from endophytic streptomyces griseoflavus P4

Amylase enzymes are currently used to accelerate starch degradation in many industrial processes. Streptomyces sp., an endophytic actinomycete, is well known as a potential source of hydrolytic enzymes, antimicrobial agents, and many secondary metabolites. Previously, an endophytic Streptomyces gris...

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Main Authors: Tang-um J., Niamsup H.
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Published: Chiang Mai University 2015
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spelling th-cmuir.6653943832-386462015-06-16T07:53:46Z Extracellular amylase activity from endophytic streptomyces griseoflavus P4 Tang-um J. Niamsup H. Physics and Astronomy (all) Chemistry (all) Materials Science (all) Mathematics (all) Biochemistry, Genetics and Molecular Biology (all) Amylase enzymes are currently used to accelerate starch degradation in many industrial processes. Streptomyces sp., an endophytic actinomycete, is well known as a potential source of hydrolytic enzymes, antimicrobial agents, and many secondary metabolites. Previously, an endophytic Streptomyces griseoflavus P4 was isolated from sweet pea root and identified by 16S rRNA sequence analysis. Using a plate assay, the S. griseoflavus P4 was found to be capable of producing amylase enzymes. The maximum amylase activity was 1.66±0.07 U/mL on the 7 th day of growth, while the total biomass was 0.085±0.005 g of dry pellet in 100 mL medium. In this work, the P4 strain exhibited a specific activity of 118.4 U/mg protein. Amylase production was found to be growth-associated and started in a log phase. Maximum enzyme production was reached during the stationary phase. The optimal conditions for activity were found to be 40 degrees C and a pH of 7. 2015-06-16T07:53:46Z 2015-06-16T07:53:46Z 2012-12-03 Article 01252526 2-s2.0-84870185402 http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84870185402&origin=inward http://cmuir.cmu.ac.th/handle/6653943832/38646 Chiang Mai University
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Physics and Astronomy (all)
Chemistry (all)
Materials Science (all)
Mathematics (all)
Biochemistry, Genetics and Molecular Biology (all)
spellingShingle Physics and Astronomy (all)
Chemistry (all)
Materials Science (all)
Mathematics (all)
Biochemistry, Genetics and Molecular Biology (all)
Tang-um J.
Niamsup H.
Extracellular amylase activity from endophytic streptomyces griseoflavus P4
description Amylase enzymes are currently used to accelerate starch degradation in many industrial processes. Streptomyces sp., an endophytic actinomycete, is well known as a potential source of hydrolytic enzymes, antimicrobial agents, and many secondary metabolites. Previously, an endophytic Streptomyces griseoflavus P4 was isolated from sweet pea root and identified by 16S rRNA sequence analysis. Using a plate assay, the S. griseoflavus P4 was found to be capable of producing amylase enzymes. The maximum amylase activity was 1.66±0.07 U/mL on the 7 th day of growth, while the total biomass was 0.085±0.005 g of dry pellet in 100 mL medium. In this work, the P4 strain exhibited a specific activity of 118.4 U/mg protein. Amylase production was found to be growth-associated and started in a log phase. Maximum enzyme production was reached during the stationary phase. The optimal conditions for activity were found to be 40 degrees C and a pH of 7.
format Article
author Tang-um J.
Niamsup H.
author_facet Tang-um J.
Niamsup H.
author_sort Tang-um J.
title Extracellular amylase activity from endophytic streptomyces griseoflavus P4
title_short Extracellular amylase activity from endophytic streptomyces griseoflavus P4
title_full Extracellular amylase activity from endophytic streptomyces griseoflavus P4
title_fullStr Extracellular amylase activity from endophytic streptomyces griseoflavus P4
title_full_unstemmed Extracellular amylase activity from endophytic streptomyces griseoflavus P4
title_sort extracellular amylase activity from endophytic streptomyces griseoflavus p4
publisher Chiang Mai University
publishDate 2015
url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84870185402&origin=inward
http://cmuir.cmu.ac.th/handle/6653943832/38646
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