A ten­der mo­ment

Know what’s your beef and what it takes to de­rive flavour­ful, ten­der and suc­cu­lent steaks.

The Star Malaysia - Star2 - - Taste - star2@thes­tar.com.my Chris Chan

ONE some­what odd dis­ad­van­tage of liv­ing in ru­ral France is, quite hon­estly, the ex­treme fresh­ness of much of the pro­duce. Wher­ever pos­si­ble, we like to get our food from lo­cal mar­kets and or­ganic stalls (or we some­times pick the fruits di­rectly from trees and bushes dur­ing the sea­sons) – this means great greens and fruits, though the down­side is that we have to eat the stuff quickly be­fore they go off due to the (mostly) un­treated na­ture of the pro­duce.

Not hav­ing a huge freezer means we can­not or­der a side of beef or lamb from a farmer – so this means weekly trips by car to get meats from the butcher in the next vil­lage.

Some­times, I pre­fer walk­ing the dis­tance of 5.5km each way there and back with a chiller bag in the ruck­sack – the scenery is lovely and the 11km walk is of­ten ex­hil­a­rat­ing (though one has to watch out for snakes in sum­mer) while an­tic­i­pat­ing the taste of home­made pates, sausages, ril­lettes de porc and other stuff on arrival home.

The bum­mer is that the butcher gets his meat fresh from lo­cal farms and this means his beef is not re­ally that aged.

Eat­ing fresh beef is gen­er­ally not ter­ri­bly en­joy­able as the mus­cle struc­ture of beef tends to be tough, even for steak cuts like ten­der­loin, and there­fore beef gen­er­ally needs age­ing to soften it – the age­ing process also de­vel­ops the de­li­cious flavours of meat.

Most of the lo­cal beef here in my ru­ral part of France is aged for only a cou­ple of weeks or less be­fore sale – and this ex­plains why dishes based on lo­cal beef are of­ten stews cooked for hours to soften the mus­cle tis­sues. This is quite re­gret­table as I usu­ally dis­like such over­cooked meat.

There is of course very good aged beef avail­able in France, but for me this in­volves a 50km trip to a big, sprawl­ing town – and although I like beef, I do not en­joy do­ing a 100km round trip to pay three or four times the price for a piece of meat.

Also, I am not such an ar­dent, picky gourmet that mak­ing such a trip makes sense, es­pe­cially if there is some sci­en­tific way to make fresh lo­cal beef taste bet­ter.

The breed mat­ters

Hav­ing lived in Lon­don for many years, my pre­ferred steaks there are rib-eyes and they tend to come from An­gus cat­tle bred mostly in Scot­land – they are suc­cu­lent, flavour­ful with a good bal­ance of fat and meat.

Trav­el­ling around Europe meant tast­ing awe­some breeds like Chi­an­ina, Sim­men­tal and Charo­lais – all stun­ningly de­li­cious meats, though the best beef in Europe might be the mas­sive rib-eyes called chuletón from the Ru­bia Gal­lega cat­tle in the Basque re­gion of Spain.

And then of course, there is the ubiq­ui­tous wagyu beef (de­rived from var­i­ous breeds), orig­i­nally from Kobe, Ja­pan and now also other coun­tries – very fine meat but per­haps a lit­tle too pre­cious for me.

Clearly, the ge­net­ics of the var­i­ous breeds mat­ter very much and there­fore good tast­ing beef is not only just about age­ing.

So to clar­ify the sit­u­a­tion, the aim of this in­ves­ti­ga­tion is to ex­am­ine ways to max­imise the best tex­ture and flavour from any breed in the short­est pos­si­ble time.

In this case, the breed avail­able at my lo­cal butcher is Li­mousin sup­plied from farms close to the re­gion – a good enough breed but per­haps not the finest in the world for din­ing. Bet­ter re­sults may well be achieved if I had ac­cess to Chi­an­ina or An­gus – but I do not.

A lit­tle aside about con­sump­tion

Although it might sound like a tri­fling first world prob­lem quib­bling about the taste of beef, in re­al­ity the sim­ple life here is rea­son­ably pleas­ant – and I am just cu­ri­ous about the bio­chem­istry of how to make steaks bet­ter.

How­ever, even here it can be seen that the global cul­ture of con­sumerism seems very much based on keep­ing peo­ple pro­foundly but vaguely dis­con­tented.

The un­stated in­sid­i­ous in­tent ap­pears to be keep­ing peo­ple dis­tract­edly dis­sat­is­fied – wear­ing down our scep­ti­cism and re­sis­tance un­til we fi­nally buy the glitzy prod­ucts or un­nec­es­sary ar­ti­fices mar­keted on TV, news­pa­pers, mag­a­zines, the in­ter­net, et cetera.

Then we find that such goods are point­less (per­haps even some­what un­healthy), can never ful­fil our ex­pec­ta­tions – and then we feel even more disen­chanted and need to buy some­thing else to com­pen­sate.

Liv­ing in a re­mote area does help to quan­tify things as it is sim­ple to use dis­tance as a mea­sure of mar­ginal util­ity or de­sir­abil­ity – thus far, it has never been worth trav­el­ling 50km to eat fried chicken or a burger, though I might eat fried chicken once ev­ery few months if there is a shop less than 100m from home.

The irony of course is that I would prob­a­bly never want to live in such a place – but we are just talk­ing ab­stract quan­tifi­ca­tion here.

The same un­sat­is­fac­tory sit­u­a­tion is also true with nutri­tion – the con­stant bom­bard­ment of “health news” keeps peo­ple con­fused, anx­ious and de­sirous of “bet­ter nutri­tion” so­lu­tions, not­with­stand­ing the prob­a­bil­ity that over 85% of such “news” is ac­tu­ally spon­sored in one way or another by var­i­ous fac­tions of the food in­dus­try.

I sup­pose the idea is to keep peo­ple mud­dled enough to keep in­gest­ing bad food while si­mul­ta­ne­ously per­suad­ing them to buy ex­pen­sive “health­ier” op­tions. Ei­ther way peo­ple just end up con­sum­ing more – and that seems to be the only thing that mat­ters.

Firstly, what is meat?

Re­turn­ing to the sub­ject, the de­sire for good meat got me look­ing into what de­fines good beef – and apart from breed, there is a very strong link be­tween how long meat has been aged af­ter slaugh­ter and the price (and there­fore by im­pli­ca­tion the taste).

So it makes sense to find out what hap­pens when beef is left to age af­ter slaugh­ter and also to in­ves­ti­gate if there are any sci­en­tific tricks to get the same tasty aged ef­fect us­ing the lim­ited re­sources avail­able in a ru­ral set­ting. This soon got very fas­ci­nat­ing in­deed.

We need to start with un­der­stand­ing what meat re­ally is – we all know it is mus­cle tis­sue of some kind and it would be use­ful to know about the types of mus­cles and how they work.

Mus­cle cells are known as my­ocytes – they range from sev­eral mil­lime­tres to over 10cm in length and be­tween 10 to 100 mi­crome­tres in width. There are three kinds of mus­cles: smooth mus­cle, car­diac mus­cle and skele­tal mus­cle – and each have very dif­fer­ent func­tions.

Smooth mus­cle is usu­ally man­aged au­tonomously; that is, without any con­scious ef­fort, and ex­am­ples are the stom­ach and in­testines. Car­diac mus­cle is another spe­cialised mus­cle found in the my­ocardium of the heart – and it for­tu­nately also func­tions au­tonomously as oth­er­wise mam­mals would have to con­tin­u­ously think about mak­ing their hearts beat, even while sleep­ing.

The only mus­cles over which mam­mals can ex­ert con­trol are the skele­tal mus­cles – which are the mus­cles mam­mals use to walk, run, chew, swim, climb trees, et cetera. They are also usu­ally the an­i­mal mus­cle (meat) that hu­mans gen­er­ally pre­fer to eat so this is what we will fo­cus on.

Mus­cles in al­most all ver­te­brates are formed of my­ofib­rils and sar­com­eres. My­ofib­rils are strands of mus­cle fi­bres made up of al­ter­nate thin and thick fil­a­ments called my­ofil­a­ments which are re­peated as pat­terns of mus­cle tis­sue along the whole length of the mus­cle fi­bre.

The thin my­ofil­a­ments are mostly made up of a pro­tein called actin bound into lit­tle col­umns by another pro­tein called neb­u­lin. In­te­gral to the thin fil­a­ments are also the pro­teins tropomyosin and a com­plex group of three pro­teins known as tro­ponin – more on this a lit­tle later.

The thick my­ofil­a­ments con­sist mainly of a pro­tein called myosin which in turn is in­ter­laced with another pro­tein titin.

As men­tioned, thin and thick strands of my­ofil­a­ments over­lap and al­ter­nate with each other along a sin­gle my­ofib­ril. Groups of my­ofib­rils in turn are or­gan­ised so that they all have their thin and thick sec­tions of my­ofil­a­ments aligned in the same di­rec­tion –

this gives rise to the pat­tern of light and dark bands seen in mus­cle tis­sue un­der a mi­cro­scope.

Each sub-sec­tion be­tween two dark bands (known as Z lines) is known as a sar­com­ere. There is also the M line, which is a ring of my­omesin pro­teins en­cir­cling the mid­dle sec­tions of thick my­ofil­a­ments.

Large group­ings of my­ofib­rils (with their thin and thick my­ofil­a­ments) be­come known as mus­cle tis­sue or meat.

Skele­tal mus­cles work due to changes in in­tra­cel­lu­lar lev­els of cal­cium in the tis­sues – in short, mus­cles con­tract when the lev­els of cal­cium in­crease and mus­cles re­lax when the cal­cium lev­els drop.

How mus­cles con­tract starts with cal­cium bind­ing to var­i­ous pro­teins in the tro­ponin group (tro­ponin C, tro­ponin T and tro­ponin I) in the thin my­ofil­a­ments – this then trig­gers three al­most si­mul­ta­ne­ous re­ac­tions.

The first cal­cium re­ac­tion af­fects tro­ponin C which then ac­ti­vates and changes the con­fig­u­ra­tion of tro­ponin I, mak­ing it ready to bind with actin.

The next re­ac­tion binds tro­ponin T to tropomyosin, form­ing an in­ter­lock­ing tro­ponin-tropomyosin struc­ture – the tropomyosin pro­tein is also bound to the myosin in the thick my­ofil­a­ment.

The last re­ac­tion fi­nally binds the tro­ponin I pro­tein from the first re­ac­tion to actin in the thin my­ofil­a­ment which then con­nects with the tro­ponin-tropomyosin struc­ture.

The net ef­fect is myosin pro­teins are in­duced to slide along actin pro­teins, and there­fore the en­tire sar­com­ere con­tracts in size – this hap­pens in the A zone and I band re­gions in the di­a­gram (right).

The H zone is the an­chor part of the sar­com­ere where there are only thick my­ofil­a­ments – the myosin pro­teins in the H zone are mostly cov­ered by actin dur­ing con­trac­tion.

Note both thin and thick my­ofil­a­ments do not change in size – the sar­com­ere is short­ened be­cause of the lat­eral move­ment of the thick my­ofil­a­ments through the thin my­ofil­a­ments and the over­all range of mus­cle con­trac­tion is mul­ti­plied by the num­ber of sar­com­eres in the strands of mus­cle tis­sue.

The con­trac­tion span of any sar­com­ere is the dif­fer­ence of the A bands and I bands nar­row­ing from their orig­i­nal lengths. The titin pro­tein at­tached to the thick my­ofil­a­ment is very stretch­able, ap­pears to pro­vide ad­di­tional elas­tic­ity to the sar­com­ere and prob­a­bly also act as a guid­ance mech­a­nism for the myosin – as an aside, titin in the largest pro­tein in the hu­man body con­sist­ing of 244 folded pro­teins.

The sim­ple way

So we now know about mus­cle pro­teins and how they are or­gan­ised in the meat we eat. One very sim­ple sug­ges­tion to soften such meat there­fore would be to use a meat ham­mer to dis­rupt the in­tegrity of the sar­com­eres as shat­ter­ing the or­gan­ised (and tough) pro­tein con­fig­u­ra­tions can only make meat more ten­der.

And this is ex­actly why cooks pound meat with jagged-edge mal­lets. For ex­am­ple, pieces of pork or veal to make schnitzels and chicken breast meat to make chicken steaks.

Grind­ing and minc­ing meat would also be another sim­ple way to soften meat; for ex­am­ple, ground pork for meat­balls or sausage fill­ings.

There­fore, at least two sim­ple so­lu­tions ex­ist (pound­ing and minc­ing) to ten­derise meat very quickly. How­ever, dis­rupt­ing the con­fig­u­ra­tion of meat pro­teins in such a vi­o­lent man­ner also changes the tex­ture em­phat­i­cally so although I do of­ten pound pieces of meat at home, this can be un­sat­is­fac­tory af­ter a while as the re­sult­ing meat of­ten tastes a lit­tle rough.

Also, this pound­ing tech­nique does not work for all cuts of meat, es­pe­cially the finer beef cuts which can dry out and roughen dur­ing cook­ing when pounded be­fore­hand.

How­ever, this tech­nique does work to some ex­tent on tough cuts like rec­tus ab­domi­nus (flank), longis­simus dorsi (chuck), su­per­fi­cial pec­toral (brisket), et cetera – as long as the meat is cut ini­tially into thin (around 1cm) slices. Pound hard and sen­si­bly, as you need to dis­rupt the tough sar­com­ere struc­tures sig­nif­i­cantly (but not to the point of de­struc­tion and mushi­ness) – and cook quickly.

Re­gard­less, my opin­ion is that if time and con­di­tions per­mit, many peo­ple would prob­a­bly, and at least oc­ca­sion­ally, pre­fer to eat prop­erly aged beef steak. Please note that there are in­ter­est­ing tech­niques to con­sid­er­ably ac­cel­er­ate the age­ing of meat – more on this later.

The age­ing of beef

Tra­di­tion­ally, beef is aged by hang­ing the car­cass in a cold room or rest­ing the meat on a slab of salt in a chiller for be­tween 28 to up to 459 days – yes, you can get served beef that has been aged over a year and a quar­ter in the United States, though in Europe the most ex­treme beef is usu­ally only aged half a year or so.

Such se­verely aged beef is al­ways from grain-fed cat­tle as it needs the ex­tra fat mar­bling in the flesh to pre­vent dry­ing out pre­ma­turely – and this is why com­mer­cial beef is usu­ally aged in vac­uum-sealed bags to re­tain the moisture (and min­imise weight loss) of lesser qual­ity meat.

Per­son­ally, I draw the aged beef line at around 55 to per­haps 70 days as beef older than this tends to freak out my taste buds in much the same way as well-hung game birds make me slightly nau­seous – there is no need to dwell on the pe­cu­liar as­pects of eat­ing flesh that is sig­nif­i­cantly on the road to pu­tre­fac­tion, de­spite en­thu­si­asts pred­i­cat­ing about its “sen­sa­tion over­load”, “flavour com­plex­ity”, “chem­i­cal as­trin­gency”, et cetera.

Beef ages due to en­zy­matic ac­tiv­ity on mus­cle fi­bres fol­lowed by the bac­te­rial break­down of pro­teins and fats. The main chem­i­cal pro­cesses in­volved are pro­te­ol­y­sis, lipol­y­sis, and ox­i­da­tion.

Pro­teins are ba­si­cally struc­tures made up of amino acids and pro­te­ol­y­sis is the de­com­po­si­tion of the elas­tic rope-like mus­cle fi­bre pro­teins into more ba­sic amino acids and polypep­tides (amino acids held to­gether by pep­tide bonds).

Left alone, pro­teins take a long time to break down and there­fore pro­te­ol­y­sis needs to be catal­ysed by sev­eral en­zymes (known as pro­teases) within the flesh it­self – there will be much more about these in­ter­est­ing en­zymes later.

Lipol­y­sis is the term used to de­fine the break­ing down of fats into glyc­erol and free fatty acids and is ini­ti­ated by other en­zymes such as li­pases within the meat – lipol­y­sis is then fur­ther pro­moted by bac­te­rial ac­tion.

The com­pounds formed by age­ing even­tu­ally re­act with oxygen in air in a process called ox­i­da­tion – this can add fur­ther taste com­plex­i­ties and aro­mas, though ox­i­da­tion can de­grade meaty flavour com­pounds such as 2-Methyl-3-Fu­ran­thiol (MFT) and also form car­bonyls (eg. ke­tones, car­boxylic acid) which tend to be rather icky-tast­ing mol­e­cules. As an aside, MFT is also pro­duced com­mer­cially and used to en­hance the meaty flavour of pro­cessed foods.

Part 2 re­views the sci­ence be­hind how to ten­derise beef by age­ing beef faster and also de­scribes the re­sults of a few ex­per­i­ments with beef at home.

(Left) A trimmed 120-day dry aged rib­eye. (Above) A 120-day dry aged rib­eye be­fore trim­ming. — Pho­tos: TheMeatCase/Visu­alHunt

Ba­sic struc­ture of skele­tal mus­cle.

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