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Articles by Rupbansraaj Bathmanathan
Total Records ( 2 ) for Rupbansraaj Bathmanathan
  Rupbansraaj Bathmanathan , Yasmin Amira Che Yahya , Mashitah Mohd Yusoff and Jaya Vejayan
  Proteases are commonly available to the dairy industry and becoming saturated in their potential for further productivity among health-conscious people, which has driven positive attention towards plant-based coagulants. This review explored the possibility of coagulant plants as an ideal choice in the development of functional dairy foods and beverages and the benefits that come along to health. Dairy products like cheese require coagulation of milk by using enzymes such as rennet either in its original state, purified or genetically modified. Animal and microbe sourced coagulants have been facing many challenges due to increasing public awareness. Plant proteases are not new and have been identified previously to have the ability to coagulate milk but plants are less explored and understood in their potentials in being a milk coagulant and fortifying the curd with useful biological activities. Currently, people are looking for functional foods that provide various health benefits when consumed rather than calorie-rich food, which causes diseases. In recent times many plants are able to coagulate milk. These particular plants have been identified as an ideal choice in the development of functional dairy foods and beverages due to their dual ability of first coagulating the milk and then fortifying the curd with biologically useful compounds.
  Jaya Vejayan , Amira Alia Zulkifli , Rupbansraaj Bathmanathan and Halijah Ibrahim
  Background and Objectives: The dairy industry is in constant search for newer milk clotting coagulants to substitute rennet due to its growing demands and controversies such as; its origin from young slaughtered animals. Kistomin (EC:3.4.24) is a protease long identified on its role to cleave platelet and fibrinogen. In this study, kistomin discovered to function as a milk coagulant and investigated for its milk clotting activities. Materials and Methods: Kistomin investigated by measuring its Milk Clotting Activity (MCA) and Proteolytic Activity (PA), optimum conditions of pH, temperature, concentrations of enzyme and calcium chloride, exposures to various chelating agents and cofactor ions. Results: The MCA of kistomin was 810.44 (SU mL1) and the PA was 1.39 (U mL1), resulted in a ratio of MCA/PA value of 583. The coagulating activity of kistomin on milk was the highest at 0.76 mg mL1 enzyme concentration, 8% (w/v) of CaCl2 concentration, the temperature of 48°C and stable over a wide range of pH 5-7 with activity peaking at pH6.5. The protease completely inhibited by EDTA and 1,10 phenanthroline verifying to be a metalloprotease. The addition of Ba2+, Mn2+ and Ca2+ significantly increased the enzyme activity but inhibited by Hg2+, Pb2+ and Fe2+ ions. Kistomin promoted extensive hydrolysis of κ-casein and low level of β-casein cleavage. Conclusion: This concluded that kistomin can be used as a milk clotting candidate for the dairy industry.
 
 
 
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