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Journal : JURNAL BIOLOGI INDONESIA

Isolats Bakteri Indigenous Penghasil Milk-Clotting Protease untuk Fermentasi Keju Rahmani, Nanik; Sari, Yana Nurita; Palupi, Nurheni Sri; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 9, No 2 (2013): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (316.729 KB) | DOI: 10.14203/jbi.v9i2.166

Abstract

The aims of this research is to isolation of bacteria that potential to produce of milk clotting protease enzymes fromfermented food that will be used as a substitute for rennet in cheese making. There are five food fermentations suchas tauco, tempeh, red oncom, sticky tape, and pickled mustard greens that are used as a source for isolation of bacteriathat could produce milk clotting protease. The results obtained four isolates proteolytic bacteria from two fermentedfood samples, three isolates bacteria from tauco (TCN 1, TCN 2, TCN 3) and one isolate from pickledmustard greens (DSN 1). Based on 16S rDNA, these isolates were identified as Bacillus sp. Bacterial isolate TCN 1has a milk clotting activity of 29.17 U/mL, whereas bacteria isolates of TCN 2, TCN 3 and DSN 1 have activities of70 U/mL achieved at the 24 hours incubation, respectively. The proteolytic activities of bacteria isolates TCN 1,TCN 2, TCN 3 and DSN 1 at the 24 hours fermentation process were 0.0117 U/mL, 0.0021 U/mL, 0.0150 U/mL,and 0.200 U/mL, respectively. The ratio of milk clotting protease activity and the proteolytic activity for bacteriaisolates TCN 1, TCN 2, TCN 3 and DSN respectively were 5402, 175000, 7292, and 3333. This showed that theenzyme from bacterial isolates TCN 2 can be used as an alternative to rennin in cheese making.Keywords: milk clotting protease, cheese, calf rennet, fermentation food
Pemurnian Parsial dan Karakterisasi Amilase dari Bakteri Laut Arthrobacter arilaitensis LBF-003 Rahmasari, Dianti; Wijanarka, Wijanarka; Pujiyanto, Sri; Rahmani, Nanik; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 12, No 1 (2016): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v12i1.2323

Abstract

Starch is an abundant carbon source in nature, and ?-amylase (1, 4-?-D-glucanohydrolase; EC 3.2.1.1), which hydrolyzes ?-1, 4-glucosidic linkage in starch-related molecules. Microbe ?-amylase production is a hydrolytic enzyme and one ofinterest in its microbial production has increased dramatically due to its wide spread use in food, textile, baking anddetergent industries in recent years. Here we report ?-amylase from marine bacterium which was purified andcharacterized, as well as analyzed its hydrolysis product on starch. The enzyme of Arthrobacter arilaitensis partiallypurified by acetone precipitation with 90% and ion exchange chromatography produced specific activity 0.25 U/mg and0.38 U/mg, and it’s purity rate increased until 1.14 fold compared with former crude extract. Purifed extracelluler amilasehad an optimum activity at temperature 50°C and pH 9.0. An apparent molecular mass was between 50-75 kDa, asestimated by zimogram electrophoresis. Hydrolysis products of this enzyme on starch were maltose, maltotriose andmaltoheptaose.Keywords: alfa amylase, marine bacterium, Arthrobacter arilaitensis, purification, charaterization
ISOLATS BAKTERI INDIGENOUS PENGHASIL MILK-CLOTTING PROTEASE UNTUK FERMENTASI KEJU Rahmani, Nanik; Sari, Yana Nurita; Palupi, Nurheni Sri; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 9, No 2 (2013): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v9i2.166

Abstract

The aims of this research is to isolation of bacteria that potential to produce of milk clotting protease enzymes fromfermented food that will be used as a substitute for rennet in cheese making. There are five food fermentations suchas tauco, tempeh, red oncom, sticky tape, and pickled mustard greens that are used as a source for isolation of bacteriathat could produce milk clotting protease. The results obtained four isolates proteolytic bacteria from two fermentedfood samples, three isolates bacteria from tauco (TCN 1, TCN 2, TCN 3) and one isolate from pickledmustard greens (DSN 1). Based on 16S rDNA, these isolates were identified as Bacillus sp. Bacterial isolate TCN 1has a milk clotting activity of 29.17 U/mL, whereas bacteria isolates of TCN 2, TCN 3 and DSN 1 have activities of70 U/mL achieved at the 24 hours incubation, respectively. The proteolytic activities of bacteria isolates TCN 1,TCN 2, TCN 3 and DSN 1 at the 24 hours fermentation process were 0.0117 U/mL, 0.0021 U/mL, 0.0150 U/mL,and 0.200 U/mL, respectively. The ratio of milk clotting protease activity and the proteolytic activity for bacteriaisolates TCN 1, TCN 2, TCN 3 and DSN respectively were 5402, 175000, 7292, and 3333. This showed that theenzyme from bacterial isolates TCN 2 can be used as an alternative to rennin in cheese making.Keywords: milk clotting protease, cheese, calf rennet, fermentation food
PEMURNIAN PARSIAL DAN KARAKTERISASI AMILASE DARI BAKTERI LAUT ARTHROBACTER ARILAITENSIS LBF-003 Rahmasari, Dianti; Wijanarka, Wijanarka; Pujiyanto, Sri; Rahmani, Nanik; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 12, No 1 (2016): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v12i1.2323

Abstract

Starch is an abundant carbon source in nature, and ?-amylase (1, 4-?-D-glucanohydrolase; EC 3.2.1.1), which hydrolyzes ?-1, 4-glucosidic linkage in starch-related molecules. Microbe ?-amylase production is a hydrolytic enzyme and one ofinterest in its microbial production has increased dramatically due to its wide spread use in food, textile, baking anddetergent industries in recent years. Here we report ?-amylase from marine bacterium which was purified andcharacterized, as well as analyzed its hydrolysis product on starch. The enzyme of Arthrobacter arilaitensis partiallypurified by acetone precipitation with 90% and ion exchange chromatography produced specific activity 0.25 U/mg and0.38 U/mg, and it?s purity rate increased until 1.14 fold compared with former crude extract. Purifed extracelluler amilasehad an optimum activity at temperature 50°C and pH 9.0. An apparent molecular mass was between 50-75 kDa, asestimated by zimogram electrophoresis. Hydrolysis products of this enzyme on starch were maltose, maltotriose andmaltoheptaose.Keywords: alfa amylase, marine bacterium, Arthrobacter arilaitensis, purification, charaterization