Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system

An alternative to relieve the symptoms of lactose intolerance is the intake of the enzyme β-galactosidase in pharmaceutical dosage forms. The ability of β-galactosidase produced by Kluyveromyces lactis and Aspergillus oryzae to hydrolyze lactose in simulated conditions of the human gastrointestinal...

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Main Authors: Alessandra Bosso, Cínthia Hoch Batista de Souza, Hélio Hiroshi Suguimoto
Format: Article
Language:English
Published: São Paulo State University (UNESP) 2015-01-01
Series:Revista de Ciências Farmacêuticas Básica e Aplicada
Subjects:
Online Access:http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/80
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author Alessandra Bosso
Cínthia Hoch Batista de Souza
Hélio Hiroshi Suguimoto
author_facet Alessandra Bosso
Cínthia Hoch Batista de Souza
Hélio Hiroshi Suguimoto
author_sort Alessandra Bosso
collection DOAJ
description An alternative to relieve the symptoms of lactose intolerance is the intake of the enzyme β-galactosidase in pharmaceutical dosage forms. The ability of β-galactosidase produced by Kluyveromyces lactis and Aspergillus oryzae to hydrolyze lactose in simulated conditions of the human gastrointestinal tract was investigated. The experiment was carried out in the optimum temperature for each enzyme activity, 40 and 55°C, respectively, and at the normal human body temperature (37°C) at concentrations of 1.5, 3.0, and 5.0 g/L (enzyme from A. oryzae) or mL/L (enzyme from K. lactis). Both enzymes were completely inactivated under simulated gastric conditions (pH 2). When the enzymes were subjected to simulated small intestine conditions (pH 7.4), lactose hydrolysis has occurred, but at 37°C the percentage was lower than that under the optimal temperatures. At concentrations of 1.5, 3.0, and 5.0 mL/L the enzyme from K. lactis hydrolyzed 76.63%, 88.91% and 94.80% of lactose at 40°C, and 55.99%, 80.91% and 81.53% at 37°C, respectively. In contrast, the enzyme from A. oryzae hydrolyzed 7.11%, 16.18% and 21.29% at 55°C, and 8.4%, 11.85% and 16.43% at 37°C. It was observed that under simulated intestinal conditions, the enzyme from K. lactis was more effective on lactose hydrolysis as compared to the enzyme from A. oryzae. Considering the findings of this study, it is extremely necessary to use an enteric coating on β-galactosidase capsules so that this enzyme is released only in the small intestine, which is its site of action, thus not suffering the action of the stomach pH.
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spelling doaj.art-42c16b441ffb4e66b636fcce15e19a8a2022-12-21T19:05:19ZengSão Paulo State University (UNESP)Revista de Ciências Farmacêuticas Básica e Aplicada1808-45322179-443X2015-01-0136180Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal systemAlessandra BossoCínthia Hoch Batista de SouzaHélio Hiroshi SuguimotoAn alternative to relieve the symptoms of lactose intolerance is the intake of the enzyme β-galactosidase in pharmaceutical dosage forms. The ability of β-galactosidase produced by Kluyveromyces lactis and Aspergillus oryzae to hydrolyze lactose in simulated conditions of the human gastrointestinal tract was investigated. The experiment was carried out in the optimum temperature for each enzyme activity, 40 and 55°C, respectively, and at the normal human body temperature (37°C) at concentrations of 1.5, 3.0, and 5.0 g/L (enzyme from A. oryzae) or mL/L (enzyme from K. lactis). Both enzymes were completely inactivated under simulated gastric conditions (pH 2). When the enzymes were subjected to simulated small intestine conditions (pH 7.4), lactose hydrolysis has occurred, but at 37°C the percentage was lower than that under the optimal temperatures. At concentrations of 1.5, 3.0, and 5.0 mL/L the enzyme from K. lactis hydrolyzed 76.63%, 88.91% and 94.80% of lactose at 40°C, and 55.99%, 80.91% and 81.53% at 37°C, respectively. In contrast, the enzyme from A. oryzae hydrolyzed 7.11%, 16.18% and 21.29% at 55°C, and 8.4%, 11.85% and 16.43% at 37°C. It was observed that under simulated intestinal conditions, the enzyme from K. lactis was more effective on lactose hydrolysis as compared to the enzyme from A. oryzae. Considering the findings of this study, it is extremely necessary to use an enteric coating on β-galactosidase capsules so that this enzyme is released only in the small intestine, which is its site of action, thus not suffering the action of the stomach pH.http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/80lactase. hydrolysis. lactose intolerance. gastrointestinal tract
spellingShingle Alessandra Bosso
Cínthia Hoch Batista de Souza
Hélio Hiroshi Suguimoto
Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
Revista de Ciências Farmacêuticas Básica e Aplicada
lactase. hydrolysis. lactose intolerance. gastrointestinal tract
title Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
title_full Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
title_fullStr Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
title_full_unstemmed Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
title_short Enzyme activity of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae on simulated conditions of human gastrointestinal system
title_sort enzyme activity of β galactosidase from kluyveromyces lactis and aspergillus oryzae on simulated conditions of human gastrointestinal system
topic lactase. hydrolysis. lactose intolerance. gastrointestinal tract
url http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/80
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