Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities

Abstract. Amfar F, Fitri L, Suhartono. 2021. Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities. Biodiversitas 22: 1564-1569. Protease is an enzyme that catalyzes the hydrolysis of peptide bonds in protein. Actinobacteria are one of bac...

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Autores principales:	FADHLIAH AMFAR, Lenni Fitri, SUHARTONO SUHARTONO
Formato:	article
Lenguaje:	EN
Publicado:	MBI & UNS Solo 2021
Materias:	actinobacteria, enzyme activity, protease, molecular identification Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/646fc0085b9a49feb75bf1b6af20fac6
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spelling	oai:doaj.org-article:646fc0085b9a49feb75bf1b6af20fac62021-11-22T00:56:36ZMolecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities1412-033X2085-472210.13057/biodiv/d220363https://doaj.org/article/646fc0085b9a49feb75bf1b6af20fac62021-03-01T00:00:00Zhttps://smujo.id/biodiv/article/view/7870https://doaj.org/toc/1412-033Xhttps://doaj.org/toc/2085-4722Abstract. Amfar F, Fitri L, Suhartono. 2021. Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities. Biodiversitas 22: 1564-1569. Protease is an enzyme that catalyzes the hydrolysis of peptide bonds in protein. Actinobacteria are one of bacterial groups that is able to produce protease. Actinobacteria are Gram-positive bacteria and mostly aerobic. This study aimed to identify protease-producing actinobacteria ATIS61 isolate using 16S rRNA gene and to characterize the protease activity. This study was experimental research, consisted of amplification and sequencing of the 16S rRNA gene, and protease activity test. The 16S rRNA gene analysis showed that ATIS61 isolate was closely related to Nocardia sp. strain 335427 with a 99.88% similarity and the result of phylogenetic tree construction was related to Nocardia farcinica strain ARS8 with Bootstrap 94%. Protease activity test showed the highest activity was on the eighth day of incubation at 0.115 U/mL. Protease activity based on temperature showed the highest activity at 40°C of 0.156 U/mL and the stability of protease towards temperature was stable at 40°C and 50°C. Protease activity showed that the highest protease activity was at pH 8 of 0.096 U/mL and the highest protease stability was also at pH 8. The addition of HgCl2 showed that it could inhibit protease activity with a value of 0.059 U/mL.FADHLIAH AMFARLenni FitriSUHARTONO SUHARTONOMBI & UNS Soloarticleactinobacteria, enzyme activity, protease, molecular identificationBiology (General)QH301-705.5ENBiodiversitas, Vol 22, Iss 3 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	actinobacteria, enzyme activity, protease, molecular identification Biology (General) QH301-705.5
spellingShingle	actinobacteria, enzyme activity, protease, molecular identification Biology (General) QH301-705.5 FADHLIAH AMFAR Lenni Fitri SUHARTONO SUHARTONO Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
description	Abstract. Amfar F, Fitri L, Suhartono. 2021. Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities. Biodiversitas 22: 1564-1569. Protease is an enzyme that catalyzes the hydrolysis of peptide bonds in protein. Actinobacteria are one of bacterial groups that is able to produce protease. Actinobacteria are Gram-positive bacteria and mostly aerobic. This study aimed to identify protease-producing actinobacteria ATIS61 isolate using 16S rRNA gene and to characterize the protease activity. This study was experimental research, consisted of amplification and sequencing of the 16S rRNA gene, and protease activity test. The 16S rRNA gene analysis showed that ATIS61 isolate was closely related to Nocardia sp. strain 335427 with a 99.88% similarity and the result of phylogenetic tree construction was related to Nocardia farcinica strain ARS8 with Bootstrap 94%. Protease activity test showed the highest activity was on the eighth day of incubation at 0.115 U/mL. Protease activity based on temperature showed the highest activity at 40°C of 0.156 U/mL and the stability of protease towards temperature was stable at 40°C and 50°C. Protease activity showed that the highest protease activity was at pH 8 of 0.096 U/mL and the highest protease stability was also at pH 8. The addition of HgCl2 showed that it could inhibit protease activity with a value of 0.059 U/mL.
format	article
author	FADHLIAH AMFAR Lenni Fitri SUHARTONO SUHARTONO
author_facet	FADHLIAH AMFAR Lenni Fitri SUHARTONO SUHARTONO
author_sort	FADHLIAH AMFAR
title	Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
title_short	Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
title_full	Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
title_fullStr	Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
title_full_unstemmed	Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities
title_sort	molecular identification of a new isolate of actinobacteria atis61 and characterization of the protease activities
publisher	MBI & UNS Solo
publishDate	2021
url	https://doaj.org/article/646fc0085b9a49feb75bf1b6af20fac6
work_keys_str_mv	AT fadhliahamfar molecularidentificationofanewisolateofactinobacteriaatis61andcharacterizationoftheproteaseactivities AT lennifitri molecularidentificationofanewisolateofactinobacteriaatis61andcharacterizationoftheproteaseactivities AT suhartonosuhartono molecularidentificationofanewisolateofactinobacteriaatis61andcharacterizationoftheproteaseactivities
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Molecular identification of a new isolate of actinobacteria ATIS61 and characterization of the protease activities

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