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Effect of Genetically Modifying the Lactococcal Proteolytic System on Ripening and Flavor Development in Cheddar Cheese

By A. McGarry, J. Law, A. Coffey, C. Daly, P. F. Fox and G. F. Fitzgerald


Three batches of six Cheddar cheeses were manufactured by using the following lactococcal strains: (i) UC317 as a control; (ii) JL3601, a proteinase-negative derivative of UC317 transformed with high-copy-number plasmid pCI3601 containing the cloned proteinase gene complex from UC317; (iii) AM312, a proteinase-negative derivative of UC317 transformed with plasmid pMG36enpr containing the neutral proteinase gene from Bacillus subtilis; (iv) AC322, JL3601 transformed with pMG36enpr; (v) AC311, UC317 transformed with plasmid pNZ1120, which contains the aminopeptidase N (pepN) gene from Lactococcus lactis subsp. lactis MG1363; and (vi) AC321, JL3601 transformed with pNZ1120. Organoleptic and chemical analyses indicated that (i) the control cheeses, which were made with UC317, were of the highest quality; (ii) cheeses made with strains harboring pCI3601 in addition to either pMG36enpr (AC322) or pNZ1120 (AC321) did not ripen in a significantly different manner than cheeses made with AM312 (containing only pMG36enpr) or AC311 (containing only pNZ1120), respectively; (iii) cheeses made with strains that overproduce pepN did not have improved body, texture, and flavor characteristics; and (iv) cheeses made with strains harboring the neutral proteinase from B. subtilis (AM312 and AC322) underwent greatly accelerated proteolysis

Topics: Physiology and Biotechnology
Year: 1994
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Provided by: PubMed Central
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