Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media

Josep Anton Feliu; Carles de Mas; Josep López-Santín

doi:10.1016/0141-0229(94)00140-M

Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media

Josep Anton Feliu, Carles de Mas, Josep López-Santín

Department of Chemistry

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

22 Citations (Scopus)

Abstract

The synthesis of the protected dipeptide BocGly-PheOMe has been carried out in an aqueous-organic two-liquid-phase system. The reaction has been catalyzed by the protease papain using trichloroethylene as organic phase with an organic phase-aqueous phase volume ratio, Vorg Vaq, of 4. The results of the present article can be summarized as follows: a) A relationship between enzyme deactivation, interfacial area, and interfacial tension is stated. The addition of 0.4% Tween 80 to the reaction system stabilized papain activity for > 50 h, overcoming the problems related to the presence of the organic solvent and shear stress due to mixing; b) undesirable parallel reactions are identified; c) the peptide yield was increased by working with a fed-batch strategy. © 1995.

Original language	English
Pages (from-to)	882-887
Journal	Enzyme and Microbial Technology
Volume	17
Issue number	10
DOIs	https://doi.org/10.1016/0141-0229(94)00140-M
Publication status	Published - 1 Jan 1995

Keywords

effect of interphase on enzymes
enzyme stability
Papain
peptide synthesis
two-liquid-phase system

Access to Document

10.1016/0141-0229(94)00140-M

Cite this

@article{e3447c75a8674e9fa9aa7d584e19fc6b,

title = "Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media",

abstract = "The synthesis of the protected dipeptide BocGly-PheOMe has been carried out in an aqueous-organic two-liquid-phase system. The reaction has been catalyzed by the protease papain using trichloroethylene as organic phase with an organic phase-aqueous phase volume ratio, Vorg Vaq, of 4. The results of the present article can be summarized as follows: a) A relationship between enzyme deactivation, interfacial area, and interfacial tension is stated. The addition of 0.4% Tween 80 to the reaction system stabilized papain activity for > 50 h, overcoming the problems related to the presence of the organic solvent and shear stress due to mixing; b) undesirable parallel reactions are identified; c) the peptide yield was increased by working with a fed-batch strategy. {\textcopyright} 1995.",

keywords = "effect of interphase on enzymes, enzyme stability, Papain, peptide synthesis, two-liquid-phase system",

author = "Feliu, {Josep Anton} and {de Mas}, Carles and Josep L{\'o}pez-Sant{\'i}n",

year = "1995",

month = jan,

day = "1",

doi = "10.1016/0141-0229(94)00140-M",

language = "English",

volume = "17",

pages = "882--887",

number = "10",

}

TY - JOUR

T1 - Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media

AU - Feliu, Josep Anton

AU - de Mas, Carles

AU - López-Santín, Josep

PY - 1995/1/1

Y1 - 1995/1/1

N2 - The synthesis of the protected dipeptide BocGly-PheOMe has been carried out in an aqueous-organic two-liquid-phase system. The reaction has been catalyzed by the protease papain using trichloroethylene as organic phase with an organic phase-aqueous phase volume ratio, Vorg Vaq, of 4. The results of the present article can be summarized as follows: a) A relationship between enzyme deactivation, interfacial area, and interfacial tension is stated. The addition of 0.4% Tween 80 to the reaction system stabilized papain activity for > 50 h, overcoming the problems related to the presence of the organic solvent and shear stress due to mixing; b) undesirable parallel reactions are identified; c) the peptide yield was increased by working with a fed-batch strategy. © 1995.

AB - The synthesis of the protected dipeptide BocGly-PheOMe has been carried out in an aqueous-organic two-liquid-phase system. The reaction has been catalyzed by the protease papain using trichloroethylene as organic phase with an organic phase-aqueous phase volume ratio, Vorg Vaq, of 4. The results of the present article can be summarized as follows: a) A relationship between enzyme deactivation, interfacial area, and interfacial tension is stated. The addition of 0.4% Tween 80 to the reaction system stabilized papain activity for > 50 h, overcoming the problems related to the presence of the organic solvent and shear stress due to mixing; b) undesirable parallel reactions are identified; c) the peptide yield was increased by working with a fed-batch strategy. © 1995.

KW - effect of interphase on enzymes

KW - enzyme stability

KW - Papain

KW - peptide synthesis

KW - two-liquid-phase system

U2 - 10.1016/0141-0229(94)00140-M

DO - 10.1016/0141-0229(94)00140-M

M3 - Article

VL - 17

SP - 882

EP - 887

IS - 10

ER -

Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media

Abstract

Keywords

Access to Document

Fingerprint

Cite this