Milk-clotting activity of cucumisin, a plant serine protease from melon fruit

Abstract

Cucumisin (EC 3.4.21.25) isolated from prince melon fruit is a plant serine protease. Its milk-clotting activity was compared with plant cysteine proteases such as papain (EC 3.4.22.2) and ficain (EC 3.4.22.3). Cucumisin was more stable than papain under the condition of pH 7.1, 37 degrees C for 24 h. The milk-clotting activity of cucumisin was the same to that of papain and was half value of that of ficain.

Caseinolytic and milk-clotting activities from Moringa oleifera flowers

“…A serine protease of Cucumis melo fruit exhibited a more stable milk-clotting activity, when compared to that of papain (Uchikoba & Kaneda, 1996). Additionally, it has been reported that a serine protease from Lactuca sativa leaves promoted clotting of skim milk as well as of milk with different fat contents (Lo Piero et al, 2002;Uchikoba & Kaneda, 1996). Aspartic protease from Oryza sativa seeds promoted cleavage of j-casein, in a pattern similar to that obtained with chymosin and pepsin (Asakura, Watanabe, Abe, & Arai, 1997), and aspartic proteases from extract of Silybum marianum flowers hydrolysed caprine and ovine milk caseins (Cavalli, Silva, Cimino, Malcata, & Priolo, 2008).…”

“…A serine protease of Cucumis melo fruit exhibited a more stable milk-clotting activity, when compared to that of papain (Uchikoba & Kaneda, 1996). Additionally, it has been reported that a serine protease from Lactuca sativa leaves promoted clotting of skim milk as well as of milk with different fat contents (Lo Piero et al, 2002;Uchikoba & Kaneda, 1996).…”

Native and Biotechnologically Engineered Plant Proteases with Industrial Applications

“…Cucumisin exhibited the same milk-clotting activity of CPs such as papain, but in addition, it produced much less bitter-tasting peptides than those formed by more typical plant CPs (Uchikoba and Kaneda 1996). Other SP enzyme, Lettucine (not included in IUBMB), from L. sativa leaves, is able to provoke a significant disorganization of the micellar structure of casein.…”

EXPLORING THE MILK-CLOTTING PROPERTIES OF EXTRACTS FROM Bromelia pinguin FRUIT

“…Pardo et al (2010), using casein as substrate, found that extracts form Asclepias fruticosa seeds exhibited a lower MCA/PA ratio (0.68) than the value reported in this study. 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.…”