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Applied and Environmental Microbiology, August 1999, p. 3540-3546, Vol. 65, No. 8
Instituto de Agroquímica y
Tecnología de Alimentos (CSIC), 46100 Burjassot, Valencia,
Spain
Received 16 November 1998/Accepted 1 April 1999
Strains of Lactobacillus plantarum originally isolated
from sausages were screened for proteinase and aminopeptidase
activities toward synthetic substrates; on the basis of that screening,
L. plantarum CRL 681 was selected for further assays on
muscle proteins. The activities of whole cells, cell extracts (CE), and
a combination of both on sarcoplasmic and myofibrillar protein extracts
were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells
generated hydrophilic peptides from both sarcoplasmic and myofibrillar
proteins. Other peptides of a hydrophobic nature resulted from the
combination of whole cells and CE. The action of both enzymatic sources
on myofibrillar proteins caused maximal increases in lysine, arginine,
and leucine, while the action of those on sarcoplasmic proteins mainly
released alanine. In general, pronounced hydrolysis of muscle proteins
required enzyme activities from whole cells in addition to those
supplied by CE.
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Characterization of Muscle Sarcoplasmic and
Myofibrillar Protein Hydrolysis Caused by Lactobacillus
plantarum


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Corresponding author. Mailing address: Instituto de
Agroquímica y Tecnología de Alimentos (CSIC), Apartado
73, 46100 Burjassot, Valencia, Spain. Phone: 34 96 3900022. Fax: 34 96 3636301. E-mail: ftoldra{at}iata.csic.es.
Permanent address: Centro de Referencia para Lactobacilos (CERELA),
Chacabuco 145, 4000 San Miguel de Tucumán, Argentina.
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