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A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods

Baldev S. Baines, Keith Brocklehurst
Biochemical Journal Feb 01, 1979, 177 (2) 541-548; DOI: 10.1042/bj1770541
Baldev S. Baines
Department of Biochemistry and Chemistry, Medical College of St. Bartholomew's Hospital, University of London, Charterhouse Square, London EC1M 6BQ, U.K.
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Keith Brocklehurst
Department of Biochemistry and Chemistry, Medical College of St. Bartholomew's Hospital, University of London, Charterhouse Square, London EC1M 6BQ, U.K.
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Abstract

A method of preparation of papain (EC 3.4.22.2) from relatively soluble types of latex of Carica papaya, including spray-dried latex produced by a controlled and relatively mild process, was devised. Spray-dried latex dissolves easily in water up to 350mg/ml at 22°C, which corresponds to approx. 230mg of protein/ml. When the usual method of preparation of crystalline papain contaminated only by its oxidation products, developed by Kimmel & Smith [J. Biol. Chem. (1954) 207, 515–531], is applied to spray-dried latex, the result is a preparation of papain heavily contaminated by chymopapains A and B (EC 3.4.22.6), and to a lesser extent by papaya peptidase A. This applies also to other types of papaya-latex currently commercially available, which, though less soluble than spray-dried latex, are more soluble than the types of latex available when the method of Kimmel & Smith (1954) was developed. This contamination is avoided by adjusting the concentration of the initial latex extract to 65mg of protein/ml (or less) before salt fractionation. For spray-dried latex this corresponds to 100mg of latex/ml. Papain isolated from spray-dried latex was characterized by using 2,2′-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as thiol-specific reactivity probes and α-N-benzoyl-l-arginine ethyl ester as substrate. Papain isolated from this source appears to have the same catalytic-centre characteristics as papain isolated previously from latex produced by harsher methods. The catalysis of the hydrolysis of α-N-benzoyl-l-arginine ethyl ester by the mixture of thiol proteinases extracted from spray-dried latex by application of the method of Kimmel & Smith (1954) appears to obey Michaelis–Menten kinetics. The presence of the other enzymes results in an increase in the value of Km and a decrease in the catalytic-centre activity (kcat.) relative to the values for the catalysis by papain.

  • © 1979 London: The Biochemical Society
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February 1979

Volume: 177 Issue: 2

Biochemical Journal: 177 (2)
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A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods
Baldev S. Baines, Keith Brocklehurst
Biochemical Journal Feb 1979, 177 (2) 541-548; DOI: 10.1042/bj1770541
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A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods
Baldev S. Baines, Keith Brocklehurst
Biochemical Journal Feb 1979, 177 (2) 541-548; DOI: 10.1042/bj1770541

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