Stability of feed enzymes in physiological conditions assayed by in vitro methods

A series of in vitro incubations were carried out to investigate the stability of two enzyme preparations in conditions similar to those in the upper gastrointestinal tract of monogastric animals. The two enzyme products, one crude xylanase from Trichoderma longibrachiatum (Multifekt K) and the othe...

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Main Authors: Johan Inborr, Anne Grönlund
Format: Article
Language:English
Published: Scientific Agricultural Society of Finland 1993-03-01
Series:Agricultural and Food Science
Online Access:https://journal.fi/afs/article/view/72479
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spelling doaj-8aae3b43d6bb4ccea59c1f8b65009f7d2020-11-24T22:40:30ZengScientific Agricultural Society of FinlandAgricultural and Food Science1459-60671795-18951993-03-0122Stability of feed enzymes in physiological conditions assayed by in vitro methodsJohan Inborr0Anne GrönlundFinnfeeds International Ltd., Market House, High Street, Marlborough, Wiltshire SNB IAA, United KingdomA series of in vitro incubations were carried out to investigate the stability of two enzyme preparations in conditions similar to those in the upper gastrointestinal tract of monogastric animals. The two enzyme products, one crude xylanase from Trichoderma longibrachiatum (Multifekt K) and the other a specifically manufactured feed enzyme (Avizyme SX®), were subjected to incubations at low and neutral pH with and without proteolytic enzymes (pepsin and pancreatin). Wheat gluten was employed together with the crude xylanase to investigate its potential as a stabilising agent. Due to the buffering effect of Avizyme SX®, incubations were carried out with (pH 2.5) and without (pH 3.2) addition of either citric or hydrochloric acid. Incubation of the crude xylanase at low pH followed by incubation at neutral pH resulted in negligible loss of xylanase activity whereas β-xylosidase recovery fell to 57 per cent of the initial value (Phttps://journal.fi/afs/article/view/72479
collection DOAJ
language English
format Article
sources DOAJ
author Johan Inborr
Anne Grönlund
spellingShingle Johan Inborr
Anne Grönlund
Stability of feed enzymes in physiological conditions assayed by in vitro methods
Agricultural and Food Science
author_facet Johan Inborr
Anne Grönlund
author_sort Johan Inborr
title Stability of feed enzymes in physiological conditions assayed by in vitro methods
title_short Stability of feed enzymes in physiological conditions assayed by in vitro methods
title_full Stability of feed enzymes in physiological conditions assayed by in vitro methods
title_fullStr Stability of feed enzymes in physiological conditions assayed by in vitro methods
title_full_unstemmed Stability of feed enzymes in physiological conditions assayed by in vitro methods
title_sort stability of feed enzymes in physiological conditions assayed by in vitro methods
publisher Scientific Agricultural Society of Finland
series Agricultural and Food Science
issn 1459-6067
1795-1895
publishDate 1993-03-01
description A series of in vitro incubations were carried out to investigate the stability of two enzyme preparations in conditions similar to those in the upper gastrointestinal tract of monogastric animals. The two enzyme products, one crude xylanase from Trichoderma longibrachiatum (Multifekt K) and the other a specifically manufactured feed enzyme (Avizyme SX®), were subjected to incubations at low and neutral pH with and without proteolytic enzymes (pepsin and pancreatin). Wheat gluten was employed together with the crude xylanase to investigate its potential as a stabilising agent. Due to the buffering effect of Avizyme SX®, incubations were carried out with (pH 2.5) and without (pH 3.2) addition of either citric or hydrochloric acid. Incubation of the crude xylanase at low pH followed by incubation at neutral pH resulted in negligible loss of xylanase activity whereas β-xylosidase recovery fell to 57 per cent of the initial value (P
url https://journal.fi/afs/article/view/72479
work_keys_str_mv AT johaninborr stabilityoffeedenzymesinphysiologicalconditionsassayedbyinvitromethods
AT annegronlund stabilityoffeedenzymesinphysiologicalconditionsassayedbyinvitromethods
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