Thermal stabilization of Aspergillus phytase by L-arginine

Sunghoon Ryu; Tae Gwan Park

doi:10.1007/BF02932480

Thermal stabilization of Aspergillus phytase by L-arginine

Sunghoon Ryu, Tae Gwan Park

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.

Original language	English
Pages (from-to)	32-34
Number of pages	3
Journal	Biotechnology and Bioprocess Engineering
Volume	3
Issue number	1
DOIs	https://doi.org/10.1007/BF02932480
State	Published - 1998
Externally published	Yes

Funding

Acknowledgement This work was supported in part by an advanced research fund from the Ministry of Agriculture and Fishery in Korea (1995).

Keywords

L-arginine
Phytase
Stability
Thermal stabilization

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10.1007/BF02932480

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title = "Thermal stabilization of Aspergillus phytase by L-arginine",

abstract = "Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.",

keywords = "L-arginine, Phytase, Stability, Thermal stabilization",

author = "Sunghoon Ryu and Park, \{Tae Gwan\}",

year = "1998",

doi = "10.1007/BF02932480",

language = "English",

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journal = "Biotechnology and Bioprocess Engineering",

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T1 - Thermal stabilization of Aspergillus phytase by L-arginine

AU - Ryu, Sunghoon

AU - Park, Tae Gwan

PY - 1998

Y1 - 1998

N2 - Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.

AB - Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.

KW - L-arginine

KW - Phytase

KW - Stability

KW - Thermal stabilization

UR - https://www.scopus.com/pages/publications/54649083140

U2 - 10.1007/BF02932480

DO - 10.1007/BF02932480

M3 - Article

AN - SCOPUS:54649083140

SN - 1226-8372

VL - 3

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EP - 34

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

IS - 1

ER -

Thermal stabilization of Aspergillus phytase by L-arginine

Abstract

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Keywords

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