Claim Missing Document
Check
Articles

Found 2 Documents
Search

Characteristics of Curds With Milk Clotting Enzyme from Indonesian Local Isolate of Lactic Acid Bacteria Putranto, Wendry; Mustopa, Apon; Mamangkey, Jendri; Aritonang, Netty
International Journal of Science, Technology & Management Vol. 1 No. 2 (2020): Juli 2020
Publisher : International Journal of Science, Technology & Management

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.46729/ijstm.v1i2.18

Abstract

To get the potential of lalcat acid bacteria isolate to produce Milk Clotting Enzyme (MCE), it is necessary to screen milk clotting activity both quantitatively and qualitatively. Through qualitative observation, the characteristics of the curd resulting from enzyme activity can be obtained. MCE is a protease that has the characteristics of milking. Based on the results of this observational research, the curd characteristic produced can be used as a benchmark to determine the length of time of fermentation and optimization of the determination of ammonium sulfate precipitation concentration. Isolate BAL shows the results of a compact curd at a fermentation time of 25 hours at 37 ℃ and the optimization results of the deposition of ammonium sulfate which shows the characteristics of a compact curd by 45% ammonium sulfate.
Purification and Characterization of Rennin Like Protease from Enterococcus faecium 1.15 Isolated from Indonesia Fermented Bakasam Putranto, Wendry; Suryaningsih, Lilis; Zaenal, Apon; Mamangkey, Jendri
International Journal of Science, Technology & Management Vol. 4 No. 4 (2023): July 2023
Publisher : Publisher Cv. Inara

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.46729/ijstm.v4i4.900

Abstract

The protease enzyme produced by Lactic Acid Bacteria (LAB) with characteristics similar to rennin is called Rennin Like Protease (RLP). The purpose of the study was to obtain information on the biochemical characteristics of RLP produced by Enterococcus faecium 1.15 as a basis for the utilization of the enzyme. The first stage of the study was observation of the growth curves and the potential of the isolates to produce RLP, biochemical characterization. Rennin Like Protease (RLP) produced by Enterococcus faecium 1.15 which has been purified using Sephadex G-50 has a molecular weight of 42 kDa with biochemical characters, with an optimum temperature of 40 ℃ and pH of 4.5. The comparison between MCA/PA with a value of 3.74 which is close to the MCA value of Calf Rennet is 1.