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All Journal Biodiversitas Journal of Biological Diversity
FIFI AFIANTI
Research Center for Biotechnology, Indonesian Institute of Sciences. Jl. Raya Jakarta-Bogor Km. 46, Cibinong, Bogor 16911, West Java, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology

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Optimum growth conditions of Lactobacillus brevis LIPI13-2-LAB131 in ?-galactosidase enzyme production Aafiyah Wahyu Nur Indah -; ROHMATUSSOLIHAT ROHMATUSSOLIHAT; WINIATI PUDJI RAHAYU; FITRI SETYONINGRUM; GUNAWAN PRIADI; FIFI AFIANTI
Biodiversitas Journal of Biological Diversity Vol. 21 No. 11 (2020)
Publisher : Society for Indonesian Biodiversity

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.13057/biodiv/d211147

Abstract

Abstract. Indah AWN, Rohmatussolihat, Rahayu WP, Setyoningrum F, Priadi G, Afianti F. 2020. Optimum growth conditions of Lactobacillus brevis LIPI13-2-LAB131 in ?-galactosidase enzyme production. Biodiversitas 21: 5403-5407. Deficiency of ?-galactosidase enzyme causes lactose to become undigested in gastrointestinal system, therefore the system needs further addition of external ?-galactosidase. The sources ?-galactosidase enzyme varies from plants, animals, and microorganisms. In industrial applications, microorganisms have become a considered potential source of ?-galactosidase. Lactobacillus brevis LIPI13-2-LAB131 had high ?-galactosidase enzyme activity, which was 7.93 U/mL. The aim of this research was to optimize the growth condition of L. brevis LIPI13-2-LAB131 in order to produce maximum ?-galactosidase enzyme activity. This research consisted of performing optimization processes using design expert 7.0 (DX7) program with response surface methodology (RSM) and partial purification of ?-galactosidase enzyme. The results of this research showed that the optimum growth conditions of L. brevis LIPI13-2-LAB131 were in 1.48% lactose level, incubation temperature of 34.91 °C, incubation time of 48.48 hours, and 2.83% inoculum size with desirability value of 0.839. The result of enzyme purification showed that value of ?-galactosidase enzyme activity increased up to 22.88 ± 0.29 U/mL with purification yield of 11.65%.
Co-Authors Aafiyah Wahyu Nur Indah - FITRI SETYONINGRUM GUNAWAN PRIADI ROHMATUSSOLIHAT ROHMATUSSOLIHAT WINIATI PUDJI RAHAYU