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Probiotics in Fruits and Vegetables: Challenges, Legislation Issues, and Potential Health Benefits
Published in Deepak Kumar Verma, Ami R. Patel, Sudhanshu Billoria, Geetanjali Kaushik, Maninder Kaur, Microbial Biotechnology in Food Processing and Health, 2023
Mamta Thakur, Deepak Kumar Verma, Sudhanshu Billoria, H. W. Deshpande, Ami R. Patel, Geetanjali Kaushik
The lactose intolerance that is caused by the deficiency of lactase enzyme in the digestive tract exhibits the symptoms like abdominal pain and distension, flatus, and diarrhea that may occur between 30 min and 2 h after the ingestion of lactose (Li et al., 2012). The probiotic cultures mainly L. bulgaricus and S. thermophilus observed to enhance the lactose digestion by the microbial lactase activity consuming the lactose while reaching it in the intestine. If the food product has slower passage time, the probiotics will get more time for the digestion of lactose. The mice fed with L. lactis MG1363/FGZW (strain expressing food-grade ß-galactosidase) than naïve mice showed the significant alleviation of diarrhea symptoms within 6 h post-challenge and suppressed intestinal motility after lactose challenge, although there was no significant increase of ß-galactosidase activity in the small intestine (Li et al., 2012). Also, probiotics are helpful in the prevention of several kinds of diarrhea specifically the infantile and antibiotic-related diarrhea (Parvez et al., 2006) because they compete with the contagious microbes for the food and space in GIT.
Industrial Applications of Bacterial Enzymes
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Transglutaminase is an enzyme that catalyzes the polymerization process of milk proteins to get better usefulness of dairy products [83, 84]. Globally, approximately 70% of adults lack lactase in the intestine; this enzyme is essential for the digestion of lactose. Humans with lactose intolerance are unable to metabolize lactose due to the deficit of this enzyme. Lactase performs the breakdown of lactose to glucose and galactose and, consequently, proves digestive aid to milk products by enhancing the solubility and sweetness in the milk [85, 78]. Certain bacteria, like the lactic acid bacteria, Bifidobacterium and Lactobacillus, acquire β-galactosidase enzyme (i.e., bacterial lactase) that facilitate them to digest and utilize lactose [86]. So lactase availability becomes easier due to various bacterial sources [87, 88, 89]. Thus, in the absence of lactase, it is necessary to remove or minimize lactose content in the milk products for the people who do not have lactase to prevent severe tissue dehydration and diarrhea, and occasionally, consequences may be fatal [90, 91, 72]. Another benefit of milk treated with lactase is that it increases the sweetness of milk, thus eliminating the need for adding sugars in the production of flavored milk drinks. Ice cream, frozen dessert, and yogurt manufacturers generally use lactase to enhance scoop and creaminess, digestibility, and sweetness, to reduce sandiness owing to crystallization of lactose in intense preparations. Cheese prepared from milk, which is already hydrolyzed, ripens more rapidly compared to normal milk [93].
Bioprospecting Extremophiles for Sustainable Biobased Industry
Published in Pratibha Dheeran, Sachin Kumar, Extremophiles, 2022
Neha Basotra, rashika Raheja, Gaurav Sharma, Kumud Ashish Singh, Diksha Sharma, Rohit Rai, Bhupinder Singh Chadha
The class of enzymes that hydrolyze the glycosidic bond between a carbohydrate and another moiety are glycosyl hydrolases and are divided into well over 100 families. The hydrolysis of the glycosidic bond generally takes place with the use of only two amino acids—a proton donor and a nucleophile/base and results in retention or inversion of the anomeric configuration of the resulting carbohydrate. Lactase ( β-galactosidase) derived from organisms like Kluyveromyces lactis (Messia et al. 2007) is being used to make lactose-free milk and other dairy products in preventing lactose intolerance. Roughly 70% of the world’s population suffers from lactose intolerance resulting from a lack or loss of β-galactosidase activity. However, for the enzyme to be active, the temperature of the daily product must be raised (from about 5°C to 25°C). This elevation in temperature creates the potential for pathogens to grow as well as for altering the flavor profile of the milk A simple solution to both issues is to use a β-galactosidase from a psychrophile (Coker and Brenchley 2006). This enzyme would be active at low temperature and hydrolyze lactose throughout the entire process from production to shipment and storage by the consumer (Coker 2004). This approach could save significant amounts of money by eliminating the heating step as well as achieve a high percentage of lactose hydrolysis.
Production and partial purification by PEG/citrate ATPS of a β-galactosidase from the new promising isolate Cladosporium tenuissimum URM 7803
Published in Preparative Biochemistry & Biotechnology, 2021
Anderson José Paulo, Maria Carolina de Albuquerque Wanderley, Rafael José Vilela de Oliveira, Willie Anderson dos Santos Vieira, Luiz Carlos Alves, Daniela de Araújo Viana Marques, Attilio Converti, Ana Lúcia Figueiredo Porto
β-Galactosidases are produced by a large number of microorganisms such as filamentous fungi, bacteria and yeasts, but they are also found in vegetables, particularly almonds, peaches, apricots and apples, as well as in animal organs such as intestine, brain and placenta.[2] These enzymes are industrially important because they are used to (a) prevent lactose crystallization in sweetened, condensed and frozen dairy products such as ice cream and condensed milk, (b) solve problems associated with whey utilization and disposal, (c) avoid lactose intolerance complications in lactase-deficient individuals, (d) treat disorders of the gastrointestinal tract through the development of lactose-based supplements; (e) develop biosensors to be used in diagnostic tests.[3,4]
Potential of “coalho” cheese whey as lactose source for β-galactosidase and ethanol co-production by Kluyveromyces spp. yeasts
Published in Preparative Biochemistry & Biotechnology, 2020
Catherine Teixeira de Carvalho, Sérgio Dantas de Oliveira Júnior, Wildson Bernardino de Brito Lima, Fábio Gonçalves Macêdo de Medeiros, Ana Laura Oliveira de Sá Leitão, Everaldo Silvino dos Santos, Gorete Ribeiro de Macedo, Francisco Caninde de Sousa Júnior
Several strategies have been investigated for dealing with the CW waste disposal and the use of biotechnological processes figures as an interesting way of converting such by-product into a valuable feedstock.[8] Although difficult to degrade on the environment, the lactose content of CW can be used as a platform for the fermentation of value-added products such as ethanol, galactonic acid, [9] and β-galactosidase.[10] The enzyme β-galactosidase (β-gal; EC 3.2.1.23), also known as lactase, is a product of great interest and several applications in the food industry, as it is responsible for the hydrolysis of lactose glycosidic bonds.[11] In addition, to the increasing market share of lactose-free products for diet-restricted consumers,[12] β-gal is also used for the enzymatic production of food prebiotics such as lactulose and different galacto-oligosaccharides (GOS).[11,13]
Lactose-hydrolyzed milk powder: Physicochemical and technofunctional characterization
Published in Drying Technology, 2018
Tatiana Lopes Fialho, Evandro Martins, Carolina Rodrigues de Jesus Silva, Rodrigo Stephani, Guilherme Miranda Tavares, Arlan Caldas Pereira Silveira, Ítalo Tuler Perrone, Pierre Schuck, Luiz Fernando Cappa de Oliveira, Antônio Fernandes de Carvalho
Intolerance to lactose present in dairy products is characterized by the absence or low production of the enzyme β-galactosidase (lactase) in human organisms. Lactase is responsible for hydrolyzing lactose into two monosaccharides (glucose and galactose) which are then absorbed by the small intestine. If lactose hydrolysis is not performed by the organism, the sugars can ferment in the bowel colon and can cause gastrointestinal discomforts.[1]