Preparation of lactose free milk by fermentation using immobilizedSaccharomyces fragilis

Rao, B. Y. K.; Godbole, S. S.; D’Souza, S.F.

doi:10.1007/bf01087444

Cited by 22 publications

(4 citation statements)

References 8 publications

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“…Biocatalysts can be immobilized either using the isolated enzymes or the whole cells [31]. Immobilization of whole cells, due to operational facility, has been shown to be an easier alternative to immobilization of isolated enzyme.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

Up-To-Date Insight on Industrial Enzymes Applications and Global Market

Sarrouh¹,

Santos²,

Miyoshi³

et al. 2012

J Bioprocess Biotech

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Industrial and household catalysis becomes more and more dependent on enzymes. This is not surprising since enzymes are able to catalyze all kinds of chemical reactions. Enzymes with the desired activity under industrial conditions can be obtained by optimizing process conditions and by protein engineering. The use of enzymes frequently results in many benefits that cannot be obtained with traditional chemical treatment. These often include higher product quality and lower manufacturing cost, less waste and reduced energy consumption. Key factors driving the market growth include new enzyme technologies endeavoring to enhance cost efficiencies and productivity, and growing interest among consumers in substituting petrochemical products with other organic compounds such as enzymes. Other factor propelling market growth includes surging demand from textile manufacturers, animal feed producers, detergent manufacturers, pharmaceutical companies, bioethanol producers and cosmetics vendors. The present paper aims to provide a review on industrial enzymes, highlighting on recent scientific advances, current applications in diverse industrial sectors and global market.

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Section: Enzyme Immobilizationmentioning

confidence: 99%

Up-To-Date Insight on Industrial Enzymes Applications and Global Market

Sarrouh¹,

Santos²,

Miyoshi³

et al. 2012

J Bioprocess Biotech

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“…(Griffiths and Muir, 1978) have been immobilized in polyacrylamide gel. Cells of K. fragilis have been immobilized in cellulose derivatives (Weckstrom et al, 1980) and in alginate (Rao et al, 1988), while cells of E. coli have been immobilized in films and sponges cross-linked with glutaraldehyde (Petre et al, 1978). A further advantage of using whole cells is that the ~-galac tosidase tends to be more stable in the cell than when isolated and immobilized by other techniques (Griffiths and Muir, 1978).…”

Section: (B) Immobilization Of Whole Cells Containing /3-galactosidasementioning

confidence: 99%

Advanced Dairy Chemistry Volume 3

Fox¹

1997

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“…The economic interest in lactase comes from its possibilities of use in food and pharmaceutical industries, caused mainly by the deficiency of lactase in various populations [1,2], especially in East-/Southeast-Asia and black populations in Central Africa, the United States and Brazil. The treatment of milk and its derivatives with lactase reduces the content of lactose [3]. Thus, lactoseintolerant people can use products free of lactose or with low lactose content, without problems.…”

Section: Introductionmentioning

confidence: 99%

Optimization of pH, Temperature and Inoculum Ratio for the Production ofβ-D-Galactosidase byKluyveromyces marxianus Using a Lactose-free Medium

Furlan¹,

Schneider²,

Merkle³

et al. 2001

Acta Biotechnol.

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The pH, temperature and inoculum ratio for the production of β-galactosidase by Kluyveromyces marxianus CDB 002 were optimized using sugar-cane molasses (100 g/l) in a lactose-free medium. The temperature optimum was evaluated in the range from 28-37 °C. Lactase production was initiated after substrate consumption indicating a reversible enzyme inhibition or catabolic repression. The specific enzyme activity after 45 h was between 456.3 U/g cell mass (37 °C) and 733.3 U/g (34 °C), whereas the highest volumetric activity was obtained at 30 °C: 21.8 U/ml. This is generally consistent with results from other authors that used whey as a carbon source. Ethanol as a by-product reached its maximum concentration after 10-14 h (31.1-40.5 g/l), but was completely consumed afterwards. A pH of 5.5 without further control gave the best production rate for lactase (484.4 U/l × h). In this process, the pH was stable during cell growth at 5.5 and then went up to pH 7.2 after 45 h. At a fixed pH of 5.5 or 6.5, the production rates achieved 313.3 U/l × h and 233.3 U/ l × h, respectively. These results differed from those of other authors, who suggested a fixed pH at 7.0 using whey as a carbon source. There were no significant differences between inoculum ratios of 1% [v/v] and 10% [v/v] so that 1% is the preferable ratio as it is cheaper. Yeast extract (10 g/l) and peptone (20 g/l) were used as the vitamin and nitrogen source, respectively, for the studies of temperature and pH. These were substituted by corn steep liquor (100 g/l) for inoculum ratio experiments. Production of lactase using sugar cane molasses in a lactose-free medium gave better enzyme productivity rates than obtained by other authors using whey. The optimum conditions for β-galactosidase synthesis were a temperature of 30-34 °C and an inoculum ratio of 1% [v/v], an initial pH of 5.5 without any further control or a control of 5.5 during cell growth. Then the pH was raised up to 7.

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Preparation of lactose free milk by fermentation using immobilizedSaccharomyces fragilis

Cited by 22 publications

References 8 publications

Up-To-Date Insight on Industrial Enzymes Applications and Global Market

Up-To-Date Insight on Industrial Enzymes Applications and Global Market

Advanced Dairy Chemistry Volume 3

Optimization of pH, Temperature and Inoculum Ratio for the Production ofβ-D-Galactosidase byKluyveromyces marxianus Using a Lactose-free Medium

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