Effects of age and suckling on chymosin and pepsin activities in abomasums of goat kids

Zhang, Fuxin; Chen, Jinping; Yang, Feng; Li, Lin-Qiang

doi:10.1111/j.1471-0307.2005.00193.x

Cited by 5 publications

(2 citation statements)

References 12 publications

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“…Andrén and Bjorck (1986) reported that with continuous suckling, the secretion of prochymosin could last at least 6 mo. Casein in the milk is the main factor causing the secretion of prochymosin; thus, the abomasa of calves fed a CN diet contain a higher level of chymosin and a stable level of pepsin (Zhang et al, 2005). In rennet paste from ARLb lambs, the beneficial influence of supplementing the milk substitute with Lb.…”

Section: Enzyme Composition Of Lamb Rennet Pastesmentioning

confidence: 99%

Rennet Paste from Lambs Fed a Milk Substitute Supplemented with Lactobacillus acidophilus: Effects on Lipolysis in Ovine Cheese

Santillo

Quinto

Dentico

et al. 2007

Journal of Dairy Science

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The present work was undertaken to evaluate the effects of Lactobacillus acidophilus supplementation of a milk substitute on the features of lamb rennet paste used for cheese making. Lipolysis in cheese manufactured with rennet paste from lambs receiving supplemented milk was also evaluated. Lambs were subjected to 3 different feeding regimens (mother suckling, MS; artificial rearing, AR; and artificial rearing with 7 log10 cfu/mL of Lb. acidophilus supplementation of the milk substitute, ARLb) and slaughtered at 20 and 40 d of age for each feeding treatment. Abomasa of the lambs were processed to rennet paste. Microbial loads, enzymatic activities (chymosin, pepsin, and lipases), and renneting characteristics of the lamb rennet paste were determined. Free fatty acids and conjugated linoleic acids were detected in cheese at 60 d of ripening. Addition of 7 log10 cfu/mL of Lb. acidophilus to the milk substitute was carried out successfully. Total recovery of viable cells was recorded in milk supplied daily to the lambs in the ARLb group. The ARLb rennet had greater amounts of lactobacilli than did the MS or AR rennet, irrespective of the slaughter age of the lambs, and the ARLb rennet had higher concentrations of lactococci when lambs were slaughtered at 40 d of age. Chymosin and lipase activities were also higher in ARLb rennet than in MS or AR rennet from lambs slaughtered at an older age. Milk supplementation of ARLb lambs resulted in improved coagulating ability of the rennet and enhanced cheese lipolysis after 60 d of ripening. A reduction of all free fatty acids was observed in all cheeses when passing from 20 to 40 d of slaughter of the lambs. Conjugated linoleic acids were more abundant in ARLb cheeses at both 20 and 40 d. Therefore, supplementation of the milk substitute with Lb. acidophilus improved the enzymatic features of rennet and the healthful and nutritional characteristics of it the ovine cheese. Moreover, the addition of lactobacilli to the milk substitute made it possible to increase the slaughter age of lambs without detrimental effects on rennet characteristics.

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Section: Enzyme Composition Of Lamb Rennet Pastesmentioning

confidence: 99%

Rennet Paste from Lambs Fed a Milk Substitute Supplemented with Lactobacillus acidophilus: Effects on Lipolysis in Ovine Cheese

Santillo

Quinto

Dentico

et al. 2007

Journal of Dairy Science

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“…This produces oligopeptides and amino acids that are then taken up by enterocytes via specific transporters (Henning, 1985). By contrast, in the GI tract of zebrafish and suckling stage mammals, proteins are not fully digested in the lumen because of low protease activity (Henning, 1985;Robberecht et al, 1971;Rombout et al, 1985;Zhang et al, 2005). This allows antigens and maternal antibodies to be preserved and thus contribute to the development of innate and adaptive immune systems (Kulkarni and Newberry, 2019;Reinhardt, 1984).…”

Section: Introductionmentioning

confidence: 99%

Lysosome-Rich Enterocytes Mediate Protein Absorption in the Vertebrate Gut

et al. 2019

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Quantification of pepsin in rennet using a monoclonal antibody-based inhibition ELISA

Rolet-Répécaud

Arnould

Dupont

et al. 2017

LWT - Food Science and Technology

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We report here the cloning and functional analysis of a novel homologue of the mitochondrial carriers predominantly expressed in the central nervous system and referred to as BMCP1 (brain mitochondrial carrier protein-1). The predicted amino acid sequence of this novel mitochondrial carrier indicates a level of identity of 39, 31, or 30%, toward the mitochondrial oxoglutarate carrier, phosphate carrier, or adenine nucleotide translocator, respectively, and a level of identity of 34, 38, or 39% with the mitochondrial uncoupling proteins UCP1, UCP2, or UCP3, respectively. Northern analysis of mouse, rat, or human tissues demonstrated that mRNA of this novel gene is mainly expressed in brain, although it is 10-30-fold less expressed in other tissues. In situ hybridization analysis of brain showed it is particularly abundant in cortex, hippocampus, thalamus, amygdala, and hypothalamus. Chromosomal mapping indicates that BMCP1 is located on chromosome X of mice and at Xq24 in man. Expression of the protein in yeast strongly impaired growth rate. Analysis of respiration of total recombinant yeast or yeast spheroplasts and in particular of the relationship between respiratory rate and membrane potential of yeast spheroplasts revealed a marked uncoupling activity of respiration, suggesting that although BMCP1 sequence is more distant from the uncoupling proteins (UCPs), this protein could be a fourth member of the UCP family.

show abstract

Effects of age and suckling on chymosin and pepsin activities in abomasums of goat kids

Cited by 5 publications

References 12 publications

Rennet Paste from Lambs Fed a Milk Substitute Supplemented with Lactobacillus acidophilus: Effects on Lipolysis in Ovine Cheese

Rennet Paste from Lambs Fed a Milk Substitute Supplemented with Lactobacillus acidophilus: Effects on Lipolysis in Ovine Cheese

Lysosome-Rich Enterocytes Mediate Protein Absorption in the Vertebrate Gut

Quantification of pepsin in rennet using a monoclonal antibody-based inhibition ELISA

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