Milk clotting enzymes from marine resources and their role in cheese-making: A mini review

Arbita, Ariestya Arlene; Zhao, Jian

doi:10.1080/10408398.2023.2220030

Cited by 1 publication

(2 citation statements)

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“…This could be attributed to weak enzyme activity because of the use of low rennet concentrations and low incubation temperatures (4 • C), which are unsuitable for enzyme activity. It is well known that the optimum temperature for rennet enzyme activity ranges from 35 to 40 • C [19,56]. However, increasing the incubation time to 24 h led to a significant increase (p < 0.05) in the hydrodynamic diameter at 24 h of incubation.…”

Section: Hydrodynamic Diameter and Surface Chargementioning

confidence: 93%

“…Rennet, like other enzymes, has an optimum temperature for its activity. The optimum temperature for rennet activity in milk is around 35 • C to 40 • C [19]. At this range of temperatures, the enzyme chymosin is most effective at milk coagulating and provides ideal conditions for the enzyme to act on κ-CN, and when more than 85% κ-CN is hydrolyzed, it leads to coagulation or curd formation.…”

Section: Introductionmentioning

confidence: 99%

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Changes in Milk Protein Functionality at Low Temperatures and Rennet Concentrations

Hamouda,

Salunke

2024

Foods

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This study aimed to evaluate the influence of low-concentration rennet on the chemical, rheological characteristics, and protein fractions of skim milk (SM) at 4 ± 1 °C. Skimmed milk (SM) was divided into four lots of 500 mL, and diluted rennet (1:10,000) was added at different levels at 4 ± 1 °C. The treatments included control (no rennet), T1 (0.001 mL/rennet), T2 (0.01 mL rennet), and T3 (0.1 mL rennet) treatments, which were incubated for 24 h. The sampling was performed at 0, 1, 2, 6, 12, and 24 h, and the SM after incubation time was heated to 73 °C/16 s to denature the rennet enzyme. Skim milk samples (SMS) (control and rennet-added samples) were evaluated for proximate composition, capillary gel electrophoresis (CGE), hydrodynamic diameter, zeta potential, and rheology at 0, 1, 2, 6, 12, and 24 h. Foaming ability, foaming stability, water-holding capacity (WHC), oil emulsifying activity (OEA), and emulsion stability (ES) were performed at 0, 12, and 24 h of incubation time. There was a significant (p < 0.05) increase in non-proteins by 0.50% and in non-casein nitrogen by 0.81% as incubation progressed. The results showed that aggregation or curd was not formed during storage time. The CGE data indicated that increasing the rennet concentration had a significant (p < 0.05) effect on decreasing κ-CN, and breakdown increased at higher levels of rennet usage. There was a significant (p < 0.05) increase in the hydrodynamic diameter and a decrease in the zeta potential values in rennet-added samples at the end of the incubation time (24 h). The rheological results showed no changes in the storage modulus (G′), loss modulus (G″), or viscosity values. Increasing the rennet amount and storage time led to a significant (p < 0.05) decrease in the foaming ability and foaming stability and a significant (p < 0.05) increase in the oil emulsifying activity and emulsion stability of rennet-added SMS. This study concluded that milk protein functionality can be changed without aggregating or curd formation, and rennet milk can be processed.

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Section: Hydrodynamic Diameter and Surface Chargementioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%