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Journal articles on the topic 'Debittering'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

Suri, Shweta, Anupama Singh, Prabhat K. Nema, and Neetu Kumra Taneja. "A Comparative Study on the Debittering of Kinnow (Citrus reticulate L.) Peels: Microbial, Chemical, and Ultrasound-Assisted Microbial Treatment." Fermentation 8, no. 8 (August 14, 2022): 389. http://dx.doi.org/10.3390/fermentation8080389.

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Kinnow mandarin (Citrus reticulate L.) peels are a storehouse of well-known bioactive compounds, viz., polyphenols, flavonoids, carotenoids, limonoids, and tocopherol, which exhibit an effective antioxidant capacity. However, naringin is the most predominant bitter flavanone compound found in Kinnow peels that causes their bitterness. It prohibits the effective utilization of peels in food-based products. In the present study, a novel approach for the debittering of Kinnow peels has been established to tackle this problem. A comparative evaluation of the different debittering methods (chemical, microbial, and ultrasound-assisted microbial treatments) used on Kinnow peel naringin and bioactive compounds was conducted. Among the chemical and microbial method; solid-state fermentation with A. niger led to greater extraction of naringin content (7.08 mg/g) from kinnow peels. Moreover, the numerical process optimization of ultrasound-assisted microbial debittering was performed by the Box–Behnken design (BBD) of a response surface methodology to maximize naringin hydrolysis. Among all three debittering methods, ultrasound-assisted microbial debittering led to a greater hydrolysis of naringin content and reduced processing time. The optimum conditions were ultrasound temperature (40 °C), time (30 min), and A. niger koji extract (1.45%) for the maximum extraction rate of naringin (11.91 mg/g). These debittered Kinnow peels can be utilized as raw material to develop therapeutic food products having a high phytochemical composition without any off-flavors or bitterness.

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2

Saha, Badal C., and Kiyoshi Hayashi. "Debittering of protein hydrolyzates." Biotechnology Advances 19, no. 5 (September 2001): 355–70. http://dx.doi.org/10.1016/s0734-9750(01)00070-2.

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3

Izawa, Noboru, Ken Tokuyasu, and Kiyoshi Hayashi. "Debittering of Protein Hydrolysates UsingAeromonascaviaeAminopeptidase." Journal of Agricultural and Food Chemistry 45, no. 3 (March 1997): 543–45. http://dx.doi.org/10.1021/jf960784t.

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4

Özdemir, Yasin, Engin Güven, and Aysun Öztürk. "Debittering of Olives by Semi Drying." Pamukkale University Journal of Engineering Sciences 21, no. 9 (2015): 390–93. http://dx.doi.org/10.5505/pajes.2015.98159.

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5

Brenes, M., E. Ramírez, P. García, E. Medina, A. de Castro, and C. Romero. "New developments in table olive debittering." Acta Horticulturae, no. 1199 (April 2018): 483–88. http://dx.doi.org/10.17660/actahortic.2018.1199.77.

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6

García, Aranzazu, Concepcion Romero, Eduardo Medina, Pedro García, Antonio de Castro, and Manuel Brenes. "Debittering of Olives by Polyphenol Oxidation." Journal of Agricultural and Food Chemistry 56, no. 24 (December 24, 2008): 11862–67. http://dx.doi.org/10.1021/jf802967y.

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7

Habibi, Maryam, Mohammad Taghi Golmakani, Gholamreza Mesbahi, Mahsa Majzoobi, and Asgar Farahnaky. "Ultrasound-accelerated debittering of olive fruits." Innovative Food Science & Emerging Technologies 31 (October 2015): 105–15. http://dx.doi.org/10.1016/j.ifset.2015.06.014.

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8

Ramírez, Eva, Pedro García-García, Antonio de Castro, Concepción Romero, and Manuel Brenes. "Debittering of black dry-salted olives." European Journal of Lipid Science and Technology 115, no. 11 (September 17, 2013): 1319–24. http://dx.doi.org/10.1002/ejlt.201300167.

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9

FitzGerald, R. J., and G. O'Cuinn. "Enzymatic debittering of food protein hydrolysates." Biotechnology Advances 24, no. 2 (March 2006): 234–37. http://dx.doi.org/10.1016/j.biotechadv.2005.11.002.

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10

Kopsidas, Gerassimos C. "A regression analysis on the green olives debittering." Grasas y Aceites 42, no. 6 (December 30, 1991): 401–3. http://dx.doi.org/10.3989/gya.1991.v42.i6.1200.

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11

GARCÍA, P. GARCÍA, C. ROMERO BARRANCO, M. C. DURÁN QUINTANA, and A. GARRIDO FERNÁNDEZ. "Biogenic Amine Formation and “Zapatera” Spoilage of Fermented Green Olives: Effect of Storage Temperature and Debittering Process." Journal of Food Protection 67, no. 1 (January 1, 2004): 117–23. http://dx.doi.org/10.4315/0362-028x-67.1.117.

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The effects of temperature and the debittering process on amine formation and other chemical changes related to “zapatera” spoilage of fermented green table olives during storage, without any chemical correction, were studied. Unwashed olive brines were more concentrated in all analyzed compounds, except NaCl. No changes in formic, acetic, and succinic acids or in ethanol, hydroxytyrosol, or tyrosol were observed in the olive brines during storage. The concentration of putrescine in the brine at the beginning of storage and end of fermentation was about 38 mg/liter, and it did not change during storage. This amine only seems to be produced during the active fermentation phase. The effects of temperature and the type of debittering process and time and its interactions (except the time × temperature × debittering process on pH) had signi cant effects on the production of cadaverine and tyramine, as well as on changes of pH and lactic and propionic acids. Storage at 15°C produced a complete stabilization of the fermented olives. However, storage of washed olives at 20 and 28°C produced a gradual decrease of lactic acid content, an increase in pH, production of propionic acid, and formation of cadaverine and tyramine, the effect becoming greater as the temperature rose. It appears that formation of cadaverine and tyramine only occurs during storage and might be related to zapatera spoilage. Changes were always significantly lower in unwashed olives, which leads to a practical stabilization of the product.

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12

Sami, Parichehr S., R. B. Toma, D. B. Nelson, and Gail C. Frank. "Effects of debittering on grapefruit juice acceptance." International Journal of Food Sciences and Nutrition 48, no. 4 (January 1997): 237–42. http://dx.doi.org/10.3109/09637489709028567.

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13

Carvajal-Larenas, F. E., A. R. Linnemann, M. J. R. Nout, M. Koziol, and M. A. J. S. van Boekel. "Lupinus mutabilis: Composition, Uses, Toxicology, and Debittering." Critical Reviews in Food Science and Nutrition 56, no. 9 (June 8, 2015): 1454–87. http://dx.doi.org/10.1080/10408398.2013.772089.

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14

YEOM, HAE, KANG SUNG KIM, and JOON SHICK RHEE. "Soy Protein Hydrolysate Debittering by Lysine-Acetylation." Journal of Food Science 59, no. 5 (September 1994): 1123–26. http://dx.doi.org/10.1111/j.1365-2621.1994.tb08206.x.

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15

Shehata, Abeer Nasr, and Abeer Abas Abd El Aty. "Optimization of Process Parameters by Statistical Experimental Designs for the Production of Naringinase Enzyme by Marine Fungi." International Journal of Chemical Engineering 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/273523.

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Naringinase has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose and prunin and debittering of citrus fruit juices. Screening of fifteen marine-derived fungi, locally isolated from Ismalia, Egypt, for naringinase enzyme production, indicated thatAspergillus nigerwas the most promising. In solid state fermentation (SSF) of the agroindustrial waste, orange rind was used as a substrate containing naringin. Sequential optimization strategy, based on statistical experimental designs, was employed to enhance the production of the debittering naringinase enzyme. Effects of 19 variables were examined for their significance on naringinase production using Plackett-Burman factorial design. Significant parameters were further investigated using Taguchi’s (L1645) orthogonal array design. Based on statistical analysis (ANOVA), the optimal combinations of the major constituents of media for maximal naringinase production were evaluated as follows: 15 g orange rind waste, 30 mL moisture content, 1% grape fruit, 1% NaNO3, 0.5% KH2PO4, 5 mM MgSO4, 5 mM FeSO4, and the initial pH 7.5. The activity obtained was more than 3.14-fold the basal production medium.

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16

KIMBALL, D. A. "Debittering of Citrus Juices Using Supercritical Carbon Dioxide." Journal of Food Science 52, no. 2 (March 1987): 481–82. http://dx.doi.org/10.1111/j.1365-2621.1987.tb06644.x.

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17

Tamura, Masahiro, Naoko Mori, Takafumi Miyoshi, Shunsuke Koyama, Hideaki Kohri, and Hideo Okai. "Practical Debittering Using Model Peptides and Related Compounds." Agricultural and Biological Chemistry 54, no. 1 (January 1990): 41–51. http://dx.doi.org/10.1080/00021369.1990.10869906.

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18

Izawa, Noboru, Satoru Ishikawa, Tadayuki Tanokura, Kiyoshi Ohta, and Kiyoshi Hayashi. "Purification and Characterization ofAeromonas caviaeAminopeptidase Possessing Debittering Activity." Journal of Agricultural and Food Chemistry 45, no. 12 (December 1997): 4897–902. http://dx.doi.org/10.1021/jf970453w.

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19

Lee, H. S., and J. G. Kim. "Effects of debittering on red grapefruit juice concentrate." Food Chemistry 82, no. 2 (August 2003): 177–80. http://dx.doi.org/10.1016/s0308-8146(02)00280-7.

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20

LIN, SHIH-BIN, LYNN P. NELLES, CHRISTOPHER T. CORDLE, and RONALD L. THOMAS. "Debittering Casein Hydrolysates with Octadecyl-Siloxane (C18) Columns." Journal of Food Science 62, no. 4 (July 1997): 665–70. http://dx.doi.org/10.1111/j.1365-2621.1997.tb15431.x.

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21

Ramírez, Eva, Eduardo Medina, Pedro García, Manuel Brenes, and Concepción Romero. "Optimization of the natural debittering of table olives." LWT 77 (April 2017): 308–13. http://dx.doi.org/10.1016/j.lwt.2016.11.071.

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22

Nand, K. "Debittering of spent brewer's yeast for food purposes." Food / Nahrung 31, no. 2 (1987): 127–31. http://dx.doi.org/10.1002/food.19870310208.

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23

Prakash, S., R?S Singhal, and P?R Kulkarni. "Enzymic debittering of Indian grapefruit (Citrus paradisi) juice." Journal of the Science of Food and Agriculture 82, no. 4 (2002): 394–97. http://dx.doi.org/10.1002/jsfa.1059.

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24

Suh, Hyung Joo, Song Hwan Bae, and Dong Ouk Noh. "Debittering of corn gluten hydrolysate with active carbon." Journal of the Science of Food and Agriculture 80, no. 5 (April 2000): 614–18. http://dx.doi.org/10.1002/(sici)1097-0010(200004)80:5<614::aid-jsfa580>3.0.co;2-l.

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25

El Abboudi, M., M. El Soda, N. F. Olson, and S. Pandian. "Poster C5 Peptide hydrolase systems of debittering and non debittering strains of L. casei and partial purification of their aminopeptidases." International Dairy Journal 3, no. 4-6 (January 1993): 562–63. http://dx.doi.org/10.1016/0958-6946(93)90046-3.

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26

Zullo, Biagi Angelo, Silverio Pachioli, and Gino Ciafardini. "Reducing the Bitter Taste of Virgin Olive Oil Don Carlo by Microbial and Vegetable Enzymes Linked to the Colloidal Fraction." Colloids and Interfaces 4, no. 1 (February 28, 2020): 11. http://dx.doi.org/10.3390/colloids4010011.

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Bitter taste is a positive sensory attribute that correlates with the concentration of phenols in olive oil. However, excessive bitterness can be perceived by consumers as a negative attribute. The aim of this investigation was to improve the process of debittering Don Carlo extra virgin olive oil (EVOO), which is rich in phenols, through blending with newly produced Leccino EVOOs, which can provide high oleuropeinolytic activity. The debittering process of blending Don Carlo EVOO with two types of Leccino EVOOs (decanter and settled EVOO), was carried out during three months of storage in canisters placed in fixed positions, or periodically inverted to prevent sedimentation. The reduction in phenolic concentration and bitterness index (K225 value) reached maximum values of 51% and 42% respectively in Don Carlo EVOO mixed with Leccino settled EVOO after three months of storage in periodically inverted containers. Analytical indices and sensory analysis, in accord with bitterness index (K225) results, confirmed a reduction or elimination of bitter taste in the oil samples depending on the type of Leccino EVOO added, and the sample storage method. All analytical results remained within parameters established by the European Community regulations for commercial merceological class EVOO.

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27

Tchorbanov, Bozhidar, Margarita Marinova, and Lydia Grozeva. "Debittering of Protein Hydrolysates by Lactobacillus LBL-4 Aminopeptidase." Enzyme Research 2011 (August 24, 2011): 1–7. http://dx.doi.org/10.4061/2011/538676.

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Yoghurt strain Lactobacillus LBL-4 cultivated for 8–10 h at pH ~6.0 was investigated as a considerable food-grade source of intracellular aminopeptidase. Cell-free extract manifesting >200 AP U/l was obtained from cells harvested from 1 L culture media. Subtilisin-induced hydrolysates of casein, soybean isolate, and Scenedesmus cell protein with degree of hydrolysis 20–22% incubated at 45∘C for 10 h by 10 AP U/g peptides caused an enlarging of DH up to 40–42%, 46–48%, and 38–40% respectively. The DH increased rapidly during the first 4 h, but gel chromatography studies on BioGel P-2 showed significant changes occurred during 4–10 h of enzyme action when the DH increased gradually. After the digestion, the remained AP activity can be recovered by ultrafiltration (yield 40–50%). Scenedesmus protein hydrolysate with DH 20% was inoculated by Lactobacillus LBL-4 cells, and after 72 h cultivation the DH reached 32%. The protein hydrolysates (DH above 40%) obtained from casein and soybean isolate (high Q value) demonstrated a negligible bitterness while Scenedesmus protein hydrolysates (low Q value) after both treatments were free of bitterness.

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28

KIMBALL, DAN A., and SETH I. NORMAN. "Changes in California Naval Orange Juice during Commercial Debittering." Journal of Food Science 55, no. 1 (January 1990): 273–74. http://dx.doi.org/10.1111/j.1365-2621.1990.tb06075.x.

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29

Puri, Munish, and Uttam Chand Banerjee. "Production, purification, and characterization of the debittering enzyme naringinase." Biotechnology Advances 18, no. 3 (May 2000): 207–17. http://dx.doi.org/10.1016/s0734-9750(00)00034-3.

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30

Huszcza, Ewa, and Agnieszka Bartmańska. "The implication of yeast in debittering of spent hops." Enzyme and Microbial Technology 42, no. 5 (April 2008): 421–25. http://dx.doi.org/10.1016/j.enzmictec.2008.01.004.

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31

Fayoux, Stéphane C., Ruben J. Hernandez, and Robert V. Holland. "The Debittering of Navel Orange Juice Using Polymeric Films." Journal of Food Science 72, no. 4 (May 2007): E143—E154. http://dx.doi.org/10.1111/j.1750-3841.2007.00283.x.

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32

Damle, M. V., P. Harikumar, and S. N. Jamdar. "Debittering of protein hydrolysates using immobilized chicken intestinal mucosa." Process Biochemistry 45, no. 7 (July 2010): 1030–35. http://dx.doi.org/10.1016/j.procbio.2010.03.016.

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33

Habibi, Maryam, Mohammad-Taghi Golmakani, Asgar Farahnaky, Gholamreza Mesbahi, and Mahsa Majzoobi. "NaOH-free debittering of table olives using power ultrasound." Food Chemistry 192 (February 2016): 775–81. http://dx.doi.org/10.1016/j.foodchem.2015.07.086.

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34

Tamer, Canan Ece, Bige İncedayı, Berivan Yıldız, and Ömer Utku Çopur. "The Use of Vacuum Impregnation for Debittering Green Olives." Food and Bioprocess Technology 6, no. 12 (October 7, 2012): 3604–12. http://dx.doi.org/10.1007/s11947-012-0971-x.

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35

El Abboudi, Mouhsine, Morsi El Soda, Sithian Pandian, Michelle Barreau, Geneviève Trépanier, and Ronald E. Simard. "Peptidase activities in debittering and nondebittering strains of lactobacilli." International Dairy Journal 2, no. 1 (January 1992): 55–64. http://dx.doi.org/10.1016/0958-6946(92)90044-m.

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36

Bodakowska-Boczniewicz, Joanna, and Zbigniew Garncarek. "Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice." Molecules 24, no. 23 (November 21, 2019): 4234. http://dx.doi.org/10.3390/molecules24234234.

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Naringinase is an enzyme complex which exhibits α-l-rhamnosidase and β-d-glucosidase activity. This enzymatic complex catalyzes the hydrolysis of naringin (4′,5,7-trihydroxy flavanone 7-rhamnoglucoside), the main bittering component in grapefruit. Reduction of the level of this substance during the processing of juice has been the focus of many studies. The aim of the study was the immobilization of naringinase on chitosan microspheres activated with glutaraldehyde and, finally, the use of such immobilized enzyme for debittering grapefruit juice. The effect of naringinase concentration and characterization of the immobilized enzyme compared to the soluble enzyme were investigated. The maximum activity was observed at optimum pH 4.0 for both free and immobilized naringinase. However, the optimum temperature was shifted from 70 to 40 °C upon immobilization. The KM value of the immobilized naringinase was higher than that of soluble naringinase. The immobilization did not change the thermal stability of the enzyme. The immobilized naringinase had good operational stability. This preparation retained 88.1 ± 2.8% of its initial activity after ten runs of naringin hydrolysis from fresh grapefruit juice. The results indicate that naringinase immobilized on chitosan has potential applicability for debittering and improving the sensory properties of grapefruit juices.

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37

Muñoz, Mariela, Jessica Holtheuer, Lorena Wilson, and Paulina Urrutia. "Grapefruit Debittering by Simultaneous Naringin Hydrolysis and Limonin Adsorption Using Naringinase Immobilized in Agarose Supports." Molecules 27, no. 9 (April 30, 2022): 2867. http://dx.doi.org/10.3390/molecules27092867.

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Naringin and limonin are the two main bitter compounds of citrus products such as grapefruit juice. The aim of this investigation was to evaluate the reduction in both bitter components simultaneously using a combined biochemical and physical approach. The proposed strategy was based on the use of heterofunctional supports with glyoxyl groups that allow for the covalent immobilization of naringinase, which hydrolyses naringin and alkyl groups that allow for the adsorption of limonin. The supports were butyl-glyoxyl agarose (BGA) and octyl-glyoxyl agarose (OGA), which were characterized in terms of aldehyde group quantification and FTIR analysis. The optimal pH and temperature of free and immobilized enzymes were assessed. The maximum enzyme loading capacity of supports was analyzed. Debittering of grapefruit juice was evaluated using soluble enzyme, enzyme-free supports, and immobilized catalysts. Enzyme immobilized in BGA reduced naringin and limonin concentrations by 54 and 100%, respectively, while the use of catalyst immobilized in OGA allowed a reduction of 74 and 76%, respectively, obtaining a final concentration of both bitter components under their detection threshold. The use of OGA biocatalyst presented better results than when soluble enzyme or enzyme-free support was utilized. Biocatalyst was successfully applied in juice debittering in five repeated batches.

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38

Estivi, Lorenzo, Davide Fusi, Andrea Brandolini, and Alyssa Hidalgo. "Effect of Debittering with Different Solvents and Ultrasound on Carotenoids, Tocopherols, and Phenolics of Lupinus albus Seeds." Antioxidants 11, no. 12 (December 16, 2022): 2481. http://dx.doi.org/10.3390/antiox11122481.

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Lupin seeds represent a rich nutritional source of bioactive compounds, including antioxidant molecules such as carotenoids, tocopherols, and phenolics. However, before consumption, the lupin seeds must be debittered in order to remove their bitter and toxic alkaloids. This study analyzed the impact on the bioactive compounds of Lupinus albus seeds of a recent time- and water-saving debittering method, which employs alternative washing solutions (0.5% or 1% of either NaCl or citric acid), with or without the assistance of ultrasound. The results were compared with those of two control methods using water or a NaCl solution. The sonication, when it was significant, led to a large loss of bioactive compounds, which was most likely due to its extraction capability. The seeds that were debittered without ultrasound presented high concentrations of tocopherols (172.8–241.3 mg/kg DM), carotenoids (10.9–25.1 mg/kg DM), and soluble-free (106.9–361.1 mg/kg DM), soluble-conjugated (93.9–118.9 mg/kg DM), and insoluble-bound (59.2–156.7 mg/kg DM) phenolics. The soluble-free fraction showed the greatest loss after a prolonged treatment. Overall, debittering with citric acid or NaCl preserved the highest concentration of antioxidant compounds by shortening the treatment time, thus preventing extensive leaching.

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39

Meijer, Wilco, Bert van de Bunt, Marja Twigt, Boudewijn de Jonge, Gerrit Smit, and Jeroen Hugenholtz. "Lysis of Lactococcus lactis subsp.cremoris SK110 and Its Nisin-Immune Transconjugant in Relation to Flavor Development in Cheese." Applied and Environmental Microbiology 64, no. 5 (May 1, 1998): 1950–53. http://dx.doi.org/10.1128/aem.64.5.1950-1953.1998.

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ABSTRACT To develop a nisin-producing cheese starter, Lactococcus lactis subsp. cremoris SK110 was conjugated with transposon Tn5276-NI, which codes for nisin immunity but not for nisin production. Cheese made with transconjugant SK110::Tn5276-NI as the starter was bitter. The muropeptide of the transconjugant contained a significantly greater amount of tetrapeptides than the muropeptide of strain SK110, which could have decreased the susceptibility of the cells to lysis and thereby the release of intracellular debittering enzymes.

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40

Kourti, Maria, Maria V. Alvanou, Zoi Skaperda, Fotis Tekos, Georgios Papaefstathiou, Panagiotis Stathopoulos, and Demetrios Kouretas. "Antioxidant and DNA-Protective Activity of an Extract Originated from Kalamon Olives Debittering." Antioxidants 12, no. 2 (January 31, 2023): 333. http://dx.doi.org/10.3390/antiox12020333.

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Table olives are a major component of the Mediterranean diet and are associated with many beneficial biological activities, which are mainly related to their phenolic compounds. Olive fruit debittering process defines the quantitative and qualitative composition of table olives in biophenols. The aim of the present study was to evaluate the in vitro antioxidant capacity and DNA-protective activity of an extract originated from brine samples, according to the Greek style debbitering process of Kalamon olive fruits. The main phenolic components determined in the brine extract were hydroxytyrosol (HT), verbascoside (VERB) and tyrosol (T). The in vitro cell-free assays showed strong radical scavenging capacity from the extract, therefore antioxidant potential. At cellular level, human endothelial cells (EA.hy296) and murine myoblasts (C2C12) were treated with non-cytotoxic concentrations of the brine extract and the redox status was assessed by measuring glutathione (GSH), reactive oxygen species (ROS) and lipid peroxidation levels (TBARS). Our results show cell type specific response, exerting a hormetic reflection at endothelial cells. Finally, in both cell lines, pre-treatment with brine extract protected from H2O2-induced DNA damage. In conclusion, this is the first holistic approach highlighted table olive wastewaters from Kalamon- Greek style debittering process, as valuable source of bioactive compounds, which could have interesting implications for the development of new products in food or other industries.

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41

Hasegawa, Shin. "Limonoid debittering of citrus juices using immobilized bacterial cell systems." Food Biotechnology 1, no. 2 (January 1987): 249–61. http://dx.doi.org/10.1080/08905438709549668.

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42

Matsuoka, Hiroatsu, Yoko Fuke, Shuichi Kaminogawa, and Kunio Yamauchi. "Purification and debittering effect of aminopeptidase II from Penicillium caseicolum." Journal of Agricultural and Food Chemistry 39, no. 8 (August 1991): 1392–95. http://dx.doi.org/10.1021/jf00008a007.

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43

Kimball, Dan A., and Seth I. Norman. "Processing effects during commercial debittering of California navel orange juice." Journal of Agricultural and Food Chemistry 38, no. 6 (June 1990): 1396–400. http://dx.doi.org/10.1021/jf00096a021.

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44

Carvajal-Larenas, F. E., M. J. R. Nout, M. A. J. S. van Boekel, M. Koziol, and A. R. Linnemann. "Modelling of the aqueous debittering process of Lupinus mutabilis Sweet." LWT - Food Science and Technology 53, no. 2 (October 2013): 507–16. http://dx.doi.org/10.1016/j.lwt.2013.03.017.

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45

Li, Li, Zuo-Yi Yang, Xiao-Qun Yang, Gui-He Zhang, Shu-Ze Tang, and Feng Chen. "Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates." Journal of Industrial Microbiology & Biotechnology 35, no. 1 (October 18, 2007): 41–47. http://dx.doi.org/10.1007/s10295-007-0264-y.

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46

Kundu, Debajyoti, Sandipan Karmakar, and Rintu Banerjee. "Simultaneous debittering and clarification of enzyme mediated mixed citrus juice production." Applied Food Research 2, no. 1 (June 2022): 100031. http://dx.doi.org/10.1016/j.afres.2021.100031.

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Kumar Pegu, Bhaba. "Microbial Naringinase and its Applications in Debittering Technology –A Mini Review." Bioscience Biotechnology Research Communications 14, no. 2 (June 15, 2021): 493–98. http://dx.doi.org/10.21786/bbrc/14.2.7.

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García, José M., Khaled Yousfi, Jesús Oliva, M. Teresa García-Diaz, and M. Carmen Pérez-Camino. "Hot Water Dipping of Olives (Olea europaea) for Virgin Oil Debittering." Journal of Agricultural and Food Chemistry 53, no. 21 (October 2005): 8248–52. http://dx.doi.org/10.1021/jf050616d.

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Cocolin, Luca, Valentina Alessandria, Cristian Botta, Roberta Gorra, Francesca De Filippis, Danilo Ercolini, and Kalliopi Rantsiou. "NaOH-Debittering Induces Changes in Bacterial Ecology during Table Olives Fermentation." PLoS ONE 8, no. 7 (July 31, 2013): e69074. http://dx.doi.org/10.1371/journal.pone.0069074.

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LIN, SHIH-BIN, LYNN P. NELLES, CHRISTOPHER T. CORDLE, and RONALD L. THOMAS. "Physical Factors Related to C18 Adsorption Columns for Debittering Protein Hydrolysates." Journal of Food Science 62, no. 5 (September 1997): 946–1010. http://dx.doi.org/10.1111/j.1365-2621.1997.tb15012.x.

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