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Determination of α-amino nitrogen in pea protein hydrolysates a comparison of three.pdf

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Determination of α-amino nitrogen in pea protein hydrolysates a comparison of three

ELSEVIER Food Chemisrry, Vol. 62, No. 3, pp. 363-367, 1998 0 1998 Elsevier Science Ltd. All rights reserved Printed in Great Britain PII: SO308-8146(97)00164-7 030878146/98 $19.00+0.00 Analytical. Nutritional and Clinical Methods Section Determination of a-amino nitrogen in pea protein hydrolysates: a comparison of three analytical methods R. Panasiuk,O R. Amarowicz,“” H. Kostyra” L. Sijtsma* “Division of Food Science, Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Tuwima 10, lo-718 Olsztyn, P.O.Box 55, Poland bAgrotechnological Research Institute (ATO-DLO), Bornsesteeg 59,6708 PD Wageningen, The Netherlands (Received 3 April 1997; revised version received and accepted 13 August 1997) Three spectrophotometric methods, using 2,4,6-trinitrobenzenesulphonic acid (TNBS), o-phthaldialdehyde (OPA) or ninhydrin, for the determination of u-amino nitrogen in pea protein isolates and hydrolysates were compared. The determined amounts of a-amino nitrogen differed greatly, depending on the method used. The TNBS and OPA methods produced comparable results, whereas the data obtained with the ninhydrin method were only half of the TNBS or OPA values. Colour stability, recovery of the standard from the protein matrix and reproducibility of the results were determined. The methods showed good accuracy (SE l-3%) with recovery values of the standard (L-leucine) from the protein matrix of 91, 111 and 75% for the OPA, ninhydrin and TNBS method, respectively. 0 1998 Elsevier Science Ltd. All rights reserved. INTRODUCTION Peas are grown all over the world but pea protein is only to a limited extent used in food applications. The quality of proteins, and, thereby their utilisation can be improved by enzymatic hydrolysis. One of the pre- requisites for obtaining a standard product by enzy- matic hydrolysis of proteins is adequate control of the degree of substrate hydrolysis (DH). The DH determi- nation should be based