4.7 Article

Influence of protein concentration and coagulation temperature on rennet-induced gelation characteristics and curd microstructure

期刊

JOURNAL OF DAIRY SCIENCE
卷 102, 期 1, 页码 177-189

出版社

ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2018-15039

关键词

ultrafiltration; protein standardization; coagulation property; curd microstructure

资金

  1. Dairy Levy Trust Fund
  2. Utah Agriculture Experiment Station (Utah State University, Logan)
  3. Leprino Foods Company (Denver, CO)

向作者/读者索取更多资源

This study characterized the coagulation properties and defined the cutting window (CW; time between storage modulus values of 35 and 70 Pa) using rheometry for milk standardized to 4, 5, or 6% protein and set at 28, 32, or 36 degrees C. Milks were standardized to a protein-to-fat ratio of approximately 1 by blending ultrafiltration retentate, skim milk, and whole milk. The internal curd microstructure for selected curd samples was analyzed with transmission electron microscopy and scanning electron microscopy. Lowering the coagulation temperature caused longer rennet coagulation time and time to reach storage modulus of 35 Pa, translating into a wider CW. It also led to a lower maximum curd-firming rate (MCFR) with lower firmness at 40 min at a given protein level. Increasing protein levels resulted in the opposite effect, although without an effect on rennet coagulation time at a given temperature. On coagulation at 28 degrees C, milk with 5% protein resulted in a similar MCFR (similar to 4 Pa/min) and CW (similar to 8.25 mm) compared with milk with 4% protein at 32 degrees C, which reflects more standard conditions, whereas increasing milk to 6% protein resulted in more than doubling of the curd-firming rate (MCFR = 9.20 Pa/min) and a shorter CW (4.60 min). Gels set at 28 degrees C had lower levels of rearrangement of protein network after 40 min compared with those set at 36 degrees C. Protein levels, on the other hand, had no influence on the levels of protein network rearrangement, as indicated by loss tangent values. The internal structure of curd particles, as investigated by both scanning electron microscopy and transmission electron microscopy, appeared to have less cross-linking and smaller casein aggregates when coagulated at 28 degrees C compared with 36 degrees C, whereas varying protein levels did not show a marked effect on aggregate formation. Overall, this study showed a marked interactive effect between coagulation temperature and protein standardization of milk on coagulation properties, which subsequently requires adjustment of the CW during cheesemaking. Lowering of the coagulation temperature greatly altered the curd microstructure, with a tendency for less syneresis during cutting. Further research is required to quantify the changes in syneresis and in fat and protein losses to whey due to changes in the microstructure of curd particles arising from the different coagulation conditions applied to the protein-fortified milk.

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