2011
DOI: 10.1016/j.phytochem.2010.12.002
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Ginger rhizome as a potential source of milk coagulating cysteine protease

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Cited by 65 publications
(46 citation statements)
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“…Its higher specificity for κ-casein with increasing temperature was also reported (Huang et al, 2011). The milk clotting activity of ginger crude extract was reported to be higher than that of calf rennet and papain but lower than mucor rennet (Hashim et al, 2011a). This study was, therefore, conducted to assess the physicochemical properties and consumer acceptability of soft unripened cheese made by coagulating camel milk using ginger crude extract.…”
Section: Introductionmentioning
confidence: 76%
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“…Its higher specificity for κ-casein with increasing temperature was also reported (Huang et al, 2011). The milk clotting activity of ginger crude extract was reported to be higher than that of calf rennet and papain but lower than mucor rennet (Hashim et al, 2011a). This study was, therefore, conducted to assess the physicochemical properties and consumer acceptability of soft unripened cheese made by coagulating camel milk using ginger crude extract.…”
Section: Introductionmentioning
confidence: 76%
“…Ginger extract was used to coagulate cow milk in which the milk clotting activity was caused due to the proteolytic activity of protease enzymes (Huang et al, 2011;Hashim et al, 2011a, b). Further, Hashim et al (2011a) revealed that ginger extracted enzyme had high specificity for α-casein followed by β-casein and κ-casein and exhibited a similar affinity for κ-casein, α-casein and β-casein. Its higher specificity for κ-casein with increasing temperature was also reported (Huang et al, 2011).…”
Section: Introductionmentioning
confidence: 94%
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“…In addition, proteases found in Jacaratia curumbensis (Arruda et al 2012), Lactuca sativa (Lo Piero et al 2002) and Asclepias fruticosa (Trejo et al 2001) and Onopordon acanthium (Brutti et al 2012), Cucumis melo (Uchikoba and Kaneda, 1996) and Zingiber officinale cv. Laiwu Shandong (Hashim et al 2011) possessed high caseinolytic activity in comparison with calf chymosin limiting their application for cheesemaking. In the present study, the low MCA/PA ratio for B. pinguin extract could be due to the presence of different active proteases with different specificity, since a poor specificity increases the proteolytic activity, having a negative impact in this value and limiting its application in cheesemaking.…”
Section: Proteolytic Activity In B Pinguin Fruit Extractmentioning
confidence: 99%