Enzymes protein hydrolysis with

Plasteins ate formed from soy protein hydrolysates with a variety of microbial proteases (149). Preferred conditions for hydrolysis and synthesis ate obtained with an enzyme-to-substrate ratio of 1 100, and a temperature of 37°C for 24—72 h. A substrate concentration of 30 wt %, 80% hydrolyzed, gives an 80% net yield of plastein from the synthesis reaction. However, these results ate based on a 1% protein solution used in the hydrolysis step this would be too low for an economical process (see Microbial transformations). 

Inositol triphosphate (IP3)-gated channels are also associated with membrane-bound receptors for hormones and neurotransmitters. In this case, binding of a given substance to its receptor causes activation of another membrane-bound protein, phospholipase C. This enzyme promotes hydrolysis of phosphatidylinositol 4,5-diphosphate (PIP2) to IP3. The IP3 then diffuses to the sarcoplasmic reticulum and opens its calcium channels to release Ca++ ions from this intracellular storage site. 

In the past, dissociation of the nucleoprotein complex has been brought about by salt solutions or by heat denaturation,129 but, more recently, decomposition has been effected by hydrolysis with trypsin,126 or by the use of dodecyl sodium sulfate130 or strontium nitrate.131 Some virus nucleoproteins are decomposed by ethyl alcohol.132 This effect may be similar to that of alcohol on the ribonucleoproteins of mammalian tissues. If minced liver is denatured with alcohol, and the dried tissue powder is extracted with 10% sodium chloride, the ribonucleoproteins are decomposed to give a soluble sodium ribonucleate while the deoxyribonucleoproteins are unaffected.133 On the other hand, extraction with 10 % sodium chloride is not satisfactory unless the proteins have first been denatured with alcohol. Denaturation also serves to inactivate enzymes of the tissues which might otherwise bring about degradation of the nucleic acid during extraction. 

When the receptor interacts with its associated G protein, the conformation of the guanine-nucleotide-binding site is altered. The subunits then dissociate, and a phosphatidylinositol-specific phospholipase C (PI-PLC) is activated [5]. The subsequent hydrolysis of phosphatidylinositol bisphosphate then produces inositol triphosphate (IP3) and diacylglycerol (DAG), which are known to be secondary messengers. For example, the water soluble IP3 is released into the cell where its ultimate targets are the calcium storage organelles from which Ca2+ is released [3]. The presence of DAG in cells is known to activate the cellular enzyme protein kinase C (PKC) [6, 7], which phosphorylates a number of cellular... 

As already noted in Fig. 5.1, the ring opening of /3-lactam antibiotics is not only a major event in their interaction with bacterial enzymes, but occurs also in the mammalian body. Chemical hydrolysis in body fluids, metabolism by mammalian enzymes and interactions with plasma proteins, all influence the pharmacological activity of these antibiotics. These aspects will be considered below. We begin with the discussion of the chemical reactivity of the /3-lactam nucleus, which plays a key role in these events. 

For the SAXS studies a CBH II sample was prepared by affinity chromatography from r. reesei QM 9414 to give the enzyme in a homogeneous form 27. In SDS-PAGE the protein had a size of 58 kDa and the isoelectric point was 4.9. Glycosy-lation was estimated as 8 to 18 % 36. The molar absorptivity at 280 nm was 75 000 M xm To obtain the core protein partial proteolytic hydrolysis with papain was per-... 

Pantothenic acid occurs in foods both in the free form and bonded to coenzyme (CoA) or acyl carrier protein (ACP) therefore hydrolysis is needed to extract it totally. Since it is degraded by acid and alkaline hydrolysis, only an enzymatic digestion can be applied. Enzyme hydrolysis with papain, diastase, clarase, takadiastase, intestinal phosphatase, pigeon liver pantetheinase, or combination of them has been used. 

Extraction is commonly carried out by hydrolysis in boiling acid such as chloridric acid or sulfuric acid. To release thiamine bonded to phosphate enzyme, hydrolysis with phosphatase, alone or together with claradiastase or takadiastase, is carried out. After the enzymatic digestion, an acid treatment is applied in order to precipitate the protein and denaturate the enzymes. Ndaw et al. [603] proved that for extraction of vitamins Bj, B, and Bg, acid hydrolysis is always superfluous if the activity of the enzymes chosen is sufficiently high. SPE or column chromatography may be used in further purification, mainly to remove excess of derivatization reagents used to convert thiamine to a highly flnorescent thiochrome derivatives. lEC may be used in purification step, as well. 

Starch derived from maize, potatoes, barley, cassava or other somces must be pretreated with hydrolytic enzymes (amylases, amyloglucosidase, proteases), which carry out liquefaction, saccharification and protein hydrolysis, respectively, before it can be fermented by yeasts and other microorganisms into potable or non-potable alcohol. Enzymes can be added in the form of malt (germinated barley) or koji (germinated rice), but this is expensive. Therefore, industrial enzymes have nearly totally replaced malt and koji as enzyme sources, thereby not only improving the economics but also the predictability of the process. 

As antioxidant peptides are rarely present in marine invertebrates, they must be released from the parent protein by hydrolysis with enzymes. Various enzymes have been used to release peptides from muscle proteins. To date, different muscle proteins have been extracted, hydrolysed, and their antioxidant activities studied, which is among all invertebrate muscles the most similar to vertebrate skeletal muscle. Various studies have been conducted to investigate the antioxidant properties of hydrolysates or bioactive peptides from marine invertebrate sources like oysters... 

Removal of the hulls is important to reduce oxalic acid content, increase protein content (72) and increase digestibility (74). Sesame proteinTas low solubility, and one method of increasing solubility is with partial enzymatic hydrolysis (75,). Hydrolysis with fungal enzymes increased the soluble protein content of sesame meal from 7.21 to 64.14%, values considered comparable to those in soy due to the tempeh fermentation. Increased lysine in the hydrolysis extract was accompanied by decreased methionine. 

A cheese-like spread, which is similar to processed cheese spread, is prepared by combining hydrolyzed Swiss-or Cheddar-whey protein and cultured cream. The whey protein is precipitated by heat and acid. The granular, chalky precipitate then acquires a smooth texture by enzymatic hydrolysis with Rhozyme P-11 at 39.5 to 40.5 °C for 30 min. The product is heated to 85 °C for 15 min to inactivate the enzymes then it is homogenized and blended with an equal quantity of 45° cream culture containing Lactobacillus casei (Webb and Whittier 1970). 

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