The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque

Background: Accumulation of denture plaque can lead to pathological changes in oral mucosa, such as denture stomatitis, halitosis, and caries. Plaque matrix is mostly formed by protein (30%) and polysaccharide complexes. Thus, an alternative enzyme solution as denture cleanser is required for hydrol...

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Main Authors: Retno Indrawati, Muhammad Luthfi, Erina Fatmala Yuli Andari
Format: Article
Language:English
Published: Universitas Airlangga 2016-06-01
Series:Dental Journal: Majalah Kedokteran Gigi
Subjects:
Online Access:http://e-journal.unair.ac.id/index.php/MKG/article/view/1877
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spelling doaj-ae8662e527cb4245909c6ddebef54ab52020-11-24T23:23:18ZengUniversitas AirlanggaDental Journal: Majalah Kedokteran Gigi1978-37282442-97402016-06-01492818610.20473/j.djmkg.v49.i2.p81-862376The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaqueRetno Indrawati0Muhammad Luthfi1Erina Fatmala Yuli Andari2Faculty of Dental Medicine, Universitas Airlangga, SurabayaFaculty of Dental Medicine, Universitas Airlangga, SurabayaFaculty of Dental Medicine, Universitas Airlangga, SurabayaBackground: Accumulation of denture plaque can lead to pathological changes in oral mucosa, such as denture stomatitis, halitosis, and caries. Plaque matrix is mostly formed by protein (30%) and polysaccharide complexes. Thus, an alternative enzyme solution as denture cleanser is required for hydrolysis of denture plaque. Papain is a proteolytic enzyme hydrolyzing proteins, while β-1,3-glucanase is a hydrolase enzyme hydrolyzing polysaccharides. Purpose: This study aimed to analyze the differences of effectiveness of ß-1,3- glucanase Vigna unguiculata enzyme and papain Carica papaya enzyme in hydrolysis of denture plaque. Method: This research was a laboratory experimental research with post test only control group design. After using denture for 24 hours, the denture was soaked in a solution of 100 ml PBS, papain enzyme, and β 1-3 glucanase enzyme at a concentration of 0.5 mg/ml, 1 mg/ml, and 2 mg/ml for 10 minutes. The solution from plaque hydrolysis was soaked in PBS and vortex enzyme for 2 minutes, then soaked in ice water for 15 minutes, and centrifuged at 3000 rpm 5-10º for 10 minutes. The supernatant was separated and analyzed. Turbidity readings then were performed in spectrofotometer with a wavelength of 480 nm. Result: 2 mg/ml of ß-1,3 glucanase enzyme generated the highest values of hydrolysis with a mean percentage of 68.77% compared to papain enzyme (44.86 %). The lowest values of hydrolysis weregenerated by PBS with a mean percentage of 3.24%. Conclusion: ß-1,3-glucanase enzyme is more effective in hydrolysis of denture plaque than papain enzyme.http://e-journal.unair.ac.id/index.php/MKG/article/view/1877Papainß-1,3-glucanasedenture plaque
collection DOAJ
language English
format Article
sources DOAJ
author Retno Indrawati
Muhammad Luthfi
Erina Fatmala Yuli Andari
spellingShingle Retno Indrawati
Muhammad Luthfi
Erina Fatmala Yuli Andari
The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
Dental Journal: Majalah Kedokteran Gigi
Papain
ß-1,3-glucanase
denture plaque
author_facet Retno Indrawati
Muhammad Luthfi
Erina Fatmala Yuli Andari
author_sort Retno Indrawati
title The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
title_short The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
title_full The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
title_fullStr The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
title_full_unstemmed The differences of effectiveness of β-1,3-glukanase Vigna unguiculata and papain Carica papaya enzymes in hydrolysis of denture plaque
title_sort differences of effectiveness of β-1,3-glukanase vigna unguiculata and papain carica papaya enzymes in hydrolysis of denture plaque
publisher Universitas Airlangga
series Dental Journal: Majalah Kedokteran Gigi
issn 1978-3728
2442-9740
publishDate 2016-06-01
description Background: Accumulation of denture plaque can lead to pathological changes in oral mucosa, such as denture stomatitis, halitosis, and caries. Plaque matrix is mostly formed by protein (30%) and polysaccharide complexes. Thus, an alternative enzyme solution as denture cleanser is required for hydrolysis of denture plaque. Papain is a proteolytic enzyme hydrolyzing proteins, while β-1,3-glucanase is a hydrolase enzyme hydrolyzing polysaccharides. Purpose: This study aimed to analyze the differences of effectiveness of ß-1,3- glucanase Vigna unguiculata enzyme and papain Carica papaya enzyme in hydrolysis of denture plaque. Method: This research was a laboratory experimental research with post test only control group design. After using denture for 24 hours, the denture was soaked in a solution of 100 ml PBS, papain enzyme, and β 1-3 glucanase enzyme at a concentration of 0.5 mg/ml, 1 mg/ml, and 2 mg/ml for 10 minutes. The solution from plaque hydrolysis was soaked in PBS and vortex enzyme for 2 minutes, then soaked in ice water for 15 minutes, and centrifuged at 3000 rpm 5-10º for 10 minutes. The supernatant was separated and analyzed. Turbidity readings then were performed in spectrofotometer with a wavelength of 480 nm. Result: 2 mg/ml of ß-1,3 glucanase enzyme generated the highest values of hydrolysis with a mean percentage of 68.77% compared to papain enzyme (44.86 %). The lowest values of hydrolysis weregenerated by PBS with a mean percentage of 3.24%. Conclusion: ß-1,3-glucanase enzyme is more effective in hydrolysis of denture plaque than papain enzyme.
topic Papain
ß-1,3-glucanase
denture plaque
url http://e-journal.unair.ac.id/index.php/MKG/article/view/1877
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